HSPA5 Antibody - #BF0317

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Product: HSPA5 Antibody
Catalog: BF0317
Description: Mouse monoclonal antibody to HSPA5
Application: WB IHC ELISA
Reactivity: Human, Monkey
Mol.Wt.: 78kDa; 72kD(Calculated).
Uniprot: P11021
RRID: AB_2833777

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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, IHC 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,Monkey
Clonality:
Monoclonal [AFB1753]
Specificity:
HSPA5 antibody detects endogenous levels of total HSPA5.
RRID:
AB_2833777
Cite Format: Affinity Biosciences Cat# BF0317, RRID:AB_2833777.
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

78 kDa glucose regulated protein; 78 kDa glucose-regulated protein; AL022860; AU019543; BIP; D2Wsu141e; D2Wsu17e; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; Epididymis secretory sperm binding protein Li 89n; FLJ26106; Glucose Regulated Protein 78kDa; GRP 78; GRP-78; GRP78; GRP78_HUMAN; Heat shock 70 kDa protein 5; Heat Shock 70kDa Protein 5; Heat shock protein family A (Hsp70) member 5; HEL S 89n; Hsce70; HSPA 5; HSPA5; Immunoglobulin Heavy Chain Binding Protein; Immunoglobulin heavy chain-binding protein; mBiP; MIF2; Sez7;

Immunogens

Immunogen:

Purified recombinant fragment of human HSPA5 expressed in E. Coli.

Uniprot:

P11021(BIP_HUMAN) >>Visit HPA database.

Gene(ID):
HSPA5(3309)
Description:
When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.The HSP70 proteins are ubiquitous molecular chaparones that are found in all organisms and tissue types. Like other members of the HSP70 family, BiP is a peptide-binding ATPase that is able to differentiate native proteins from unfolded polypeptides. BiP does not bind to fully folded and assembled proteins, except in the presence of other co-chaparones. BiP is involved in a number of key mechanisms and pathways including polypeptide translocation across the endoplasmic reticulum, folding, assembly, transport of secreted or membrane proteins, and the regulation of calcium homeostasis. Although BiP is relatively abundant, marked increases in BiP occur where there is an accumulation of unfolded polypeptides. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.
Sequence:
MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL

Research Backgrounds

Function:

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.

PTMs:

AMPylated by FICD. In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).

Subcellular Location:

Endoplasmic reticulum lumen. Melanosome. Cytoplasm.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

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

The interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers.

Belongs to the heat shock protein 70 family.

Research Fields

· Genetic Information Processing > Folding, sorting and degradation > Protein export.

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

· Human Diseases > Neurodegenerative diseases > Prion diseases.

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

· Organismal Systems > Endocrine system > Thyroid hormone synthesis.

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