Calnexin Antibody - #BF0515

(2)  
Product: Calnexin Antibody
Catalog: BF0515
Description: Mouse monoclonal antibody to Calnexin
Application: WB IF/ICC ELISA
Reactivity: Human
Mol.Wt.: 90kDa; 68kD(Calculated).
Uniprot: P27824
RRID: AB_2833627

View similar products>>

   Size Price Inventory
 50ul $250 In stock
 100ul $350 In stock
 200ul $450 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors
Related Downloads
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000, IF/ICC 1:200-1:1000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFB1603]
Specificity:
Calnexin antibody detects endogenous levels of total Calnexin.
RRID:
AB_2833627
Cite Format: Affinity Biosciences Cat# BF0515, RRID:AB_2833627.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Calnexin; CALX_HUMAN; CANX; CNX; FLJ26570; Histocompatibility complex class I antigen binding protein p88; IP90; Major histocompatibility complex class I antigen-binding protein p88; p90;

Immunogens

Immunogen:

Purified recombinant fragment of human Calnexin expressed in E. Coli.

Uniprot:

P27824(CALX_HUMAN) >>Visit HPA database.

Gene(ID):
CANX(821)
Description:
This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described.
Sequence:
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE

PTMs - P27824 As Substrate

Site PTM Type Enzyme
T59 O-Glycosylation
K61 Ubiquitination
T66 O-Glycosylation
Y70 Phosphorylation
S74 Phosphorylation
R77 Methylation
T79 O-Glycosylation
S81 Phosphorylation
S86 Phosphorylation
K87 Ubiquitination
T93 Phosphorylation
K99 Ubiquitination
K103 Acetylation
K103 Ubiquitination
K110 Ubiquitination
K118 Ubiquitination
R125 Methylation
K127 Ubiquitination
K134 Acetylation
K134 Ubiquitination
K137 Acetylation
K137 Ubiquitination
K170 Ubiquitination
K182 Ubiquitination
Y185 Phosphorylation
K193 Ubiquitination
K199 Acetylation
K199 Ubiquitination
K210 Ubiquitination
T211 Phosphorylation
Y214 Phosphorylation
K217 Acetylation
K217 Ubiquitination
K227 Acetylation
K227 Ubiquitination
T228 Phosphorylation
K233 Ubiquitination
R282 Methylation
K283 Ubiquitination
K300 Ubiquitination
S362 Phosphorylation
Y379 Phosphorylation
K380 Ubiquitination
Y393 Phosphorylation
K398 Ubiquitination
K401 Ubiquitination
S431 Phosphorylation
K458 Acetylation
K458 Ubiquitination
K459 Acetylation
K459 Ubiquitination
T509 Phosphorylation
S510 Phosphorylation
Y514 Phosphorylation
K516 Ubiquitination
K525 Ubiquitination
K537 Ubiquitination
K547 Ubiquitination
S554 Phosphorylation
T562 Phosphorylation
S564 Phosphorylation
S583 Phosphorylation P27361 (MAPK3) , P06493 (CDK1)

Research Backgrounds

Function:

Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.

PTMs:

Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity).

Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins.

Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4.

Subcellular Location:

Endoplasmic reticulum membrane>Single-pass type I membrane protein. Endoplasmic reticulum. Melanosome.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated form preferentially localizes to the perinuclear rough ER (PubMed:22314232).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Interacts with MAPK3/ERK1 (By similarity). Interacts with KCNH2. Associates with ribosomes (By similarity). Interacts with SGIP1; involved in negative regulation of endocytosis (By similarity). The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins. Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1. Interacts with PPIB. Interacts with ZNRF4. Interacts with SMIM22.

(Microbial infection) Interacts with HBV large envelope protein, isoform L.

(Microbial infection) Interacts with HBV large envelope protein, isoform M; this association may be essential for isoform M proper secretion.

Family&Domains:

Belongs to the calreticulin family.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone synthesis.

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.