Product: Phospho-EPB41 (Tyr660/Tyr418) Antibody
Catalog: AF3943
Description: Rabbit polyclonal antibody to Phospho-EPB41 (Tyr660/Tyr418)
Application: ELISA(peptide)
Reactivity: Human, Mouse
Mol.Wt.: 97kD(Calculated).
Uniprot: P11171
RRID: AB_2847666

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 100ul $350 In stock
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Product Info

Source:
Rabbit
Application:
ELISA(peptide) 1:20000-1:40000
*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,Mouse
Clonality:
Polyclonal
Specificity:
Phospho-EPB41 (Tyr660/Tyr418) Antibody detects endogenous levels of EPB41 only when phosphorylated at Tyr660/418.
RRID:
AB_2847666
Cite Format: Affinity Biosciences Cat# AF3943, RRID:AB_2847666.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , 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

4.1R; 41_HUMAN; Band 4.1; E41P; EL 1; EL1; EL1 gene; Elliptocytosis 1; Elliptocytosis 1 RH linked; EPB 4.1; EPB 41; EPB4.1; Epb41; Erythrocyte membrane protein band 4.1 (elliptocytosis 1 RH linked); Erythrocyte membrane protein band 4.1; Erythrocyte surface protein band 4.1; HE; P4.1; Protein 4.1; Protein 4.1, red blood cell type;

Immunogens

Immunogen:

A synthesized peptide derived from human EPB41 around the phosphorylation site of Tyr660/418.

Uniprot:
Gene(ID):
Sequence:
MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE

PTMs - P11171 As Substrate

Site PTM Type Enzyme
S6 Phosphorylation
S14 Phosphorylation
S56 Phosphorylation
T60 Phosphorylation
T62 Phosphorylation
R77 Methylation
S80 Phosphorylation
S84 Phosphorylation
S85 Phosphorylation
S92 Phosphorylation
S95 Phosphorylation
S104 Phosphorylation
S144 Phosphorylation
S149 Phosphorylation
S151 Phosphorylation
S152 Phosphorylation
T155 Phosphorylation
S180 Phosphorylation
S188 Phosphorylation
S191 Phosphorylation
T195 Phosphorylation
S200 Phosphorylation
T220 Phosphorylation
Y222 Phosphorylation
K228 Ubiquitination
K237 Ubiquitination
K269 Ubiquitination
K361 Acetylation
K361 Methylation
K361 Ubiquitination
K366 Acetylation
K366 Ubiquitination
K372 Methylation
K372 Ubiquitination
Y374 Phosphorylation
T378 Phosphorylation
Y459 Phosphorylation
K466 Acetylation
K466 Ubiquitination
S491 O-Glycosylation
T494 Phosphorylation
K499 Ubiquitination
S505 Phosphorylation
K506 Ubiquitination
S510 Phosphorylation
S521 Phosphorylation
R526 Methylation
S540 Phosphorylation
S542 Phosphorylation
S551 Phosphorylation
S555 Phosphorylation
T559 Phosphorylation
S560 Phosphorylation
T565 Phosphorylation
S578 Phosphorylation
Y660 Phosphorylation P00533 (EGFR)
S664 Phosphorylation
S674 Phosphorylation
S684 Phosphorylation
K689 Ubiquitination
S709 Phosphorylation
T710 Phosphorylation
S712 Phosphorylation
T716 Phosphorylation
T736 Phosphorylation
K747 Ubiquitination
Y767 Phosphorylation
T786 Phosphorylation
T794 Phosphorylation
T806 Phosphorylation
K808 Ubiquitination
S812 Phosphorylation
T823 Phosphorylation
K842 Ubiquitination
S849 Phosphorylation
T851 Phosphorylation
T859 Phosphorylation

Research Backgrounds

Function:

Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

PTMs:

Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.

Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.

O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain.

Subcellular Location:

Cytoplasm>Cytoskeleton. Cytoplasm>Cell cortex. Nucleus.

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

Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Interacts with calmodulin. Interacts with CENPJ. Interacts with DLG1. Also found to associate with contractile apparatus and tight junctions. Interacts with NUMA1; this interaction is negatively regulated by CDK1 during metaphase and promotes anaphase-specific localization of NUMA1 in symmetrically dividing cells. Interacts with ATP2B1; regulates small intestinal calcium absorption through regulation of membrane expression of ATP2B1 (By similarity).

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For Research Use Only.
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