LAMB1 Antibody - #BF0229
Product: | LAMB1 Antibody |
Catalog: | BF0229 |
Description: | Mouse monoclonal antibody to LAMB1 |
Application: | WB IHC ELISA |
Reactivity: | Human |
Mol.Wt.: | 198kDa; 198kD(Calculated). |
Uniprot: | P07942 |
RRID: | AB_2833675 |
Product Info
*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.
Cite Format: Affinity Biosciences Cat# BF0229, RRID:AB_2833675.
Fold/Unfold
CLM; Cutis laxa with marfanoid phenotype; LAM B1; LAMB 1; LAMB1; LAMB1_HUMAN; Laminin B1; Laminin B1 chain; Laminin beta 1 chain; Laminin beta 1 chain precursor; Laminin beta1; Laminin subunit beta 1; Laminin subunit beta-1; Laminin-1 subunit beta; Laminin-10 subunit beta; Laminin-12 subunit beta; Laminin-2 subunit beta; Laminin-6 subunit beta; Laminin-8 subunit beta; LIS5; MGC142015;
Immunogens
Purified recombinant fragment of human LAMB1 expressed in E. Coli.
- P07942 LAMB1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGLLQLLAFSFLALCRARVRAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSISCHFDMAVYLATGNVSGGVCDDCQHNTMGRNCEQCKPFYYQHPERDIRDPNFCERCTCDPAGSQNEGICDSYTDFSTGLIAGQCRCKLNVEGEHCDVCKEGFYDLSSEDPFGCKSCACNPLGTIPGGNPCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLDGCRPCDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYYFATLDHYLYEAEEANLGPGVSIVERQYIQDRIPSWTGAGFVRVPEGAYLEFFIDNIPYSMEYDILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTIPDDDNQVVSLSPGSRYVVLPRPVCFEKGTNYTVRLELPQYTSSDSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGVVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALLHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGCKPCECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPSCQPCQCNGHADDCDPVTGECLNCQDYTMGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGYFGNPSEVGGSCQPCQCHNNIDTTDPEACDKETGRCLKCLYHTEGEHCQFCRFGYYGDALQQDCRKCVCNYLGTVQEHCNGSDCQCDKATGQCLCLPNVIGQNCDRCAPNTWQLASGTGCDPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIAELTNRTHRFLEKAKALKISGVIGPYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKCGGPGCGGLVTVAHNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTCL
PTMs - P07942 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S154 | Phosphorylation | Uniprot | |
K184 | Ubiquitination | Uniprot | |
S195 | Phosphorylation | Uniprot | |
K215 | Sumoylation | Uniprot | |
K215 | Ubiquitination | Uniprot | |
Y220 | Phosphorylation | Uniprot | |
S221 | Phosphorylation | Uniprot | |
K229 | Ubiquitination | Uniprot | |
T231 | Phosphorylation | Uniprot | |
K239 | Ubiquitination | Uniprot | |
T242 | Phosphorylation | Uniprot | |
T369 | Phosphorylation | Uniprot | |
T939 | Phosphorylation | Uniprot | |
Y950 | Phosphorylation | Uniprot | |
S953 | Phosphorylation | Uniprot | |
S1222 | Phosphorylation | Uniprot | |
K1231 | Ubiquitination | Uniprot | |
K1244 | Ubiquitination | Uniprot | |
K1255 | Ubiquitination | Uniprot | |
N1279 | N-Glycosylation | Uniprot | |
S1280 | Phosphorylation | Uniprot | |
T1281 | Phosphorylation | Uniprot | |
T1290 | Phosphorylation | Uniprot | |
K1310 | Ubiquitination | Uniprot | |
R1315 | Methylation | Uniprot | |
S1365 | Phosphorylation | Uniprot | |
T1435 | O-Glycosylation | Uniprot | |
K1476 | Ubiquitination | Uniprot | |
S1478 | Phosphorylation | Uniprot | |
S1496 | Phosphorylation | Uniprot | |
S1520 | Phosphorylation | Uniprot | |
K1611 | Ubiquitination | Uniprot | |
S1666 | Phosphorylation | Uniprot | |
Y1671 | Phosphorylation | Uniprot | |
S1682 | Phosphorylation | Uniprot | |
S1735 | Phosphorylation | Uniprot | |
K1741 | Ubiquitination | Uniprot | |
K1757 | Ubiquitination | Uniprot | |
K1773 | Ubiquitination | Uniprot |
Research Backgrounds
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.
Secreted>Extracellular space>Extracellular matrix>Basement membrane.
Note: Major component.
Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.
Research Fields
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion. (View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)
· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction. (View pathway)
· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.
· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Small cell lung cancer. (View pathway)
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