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AV44848

Sigma-Aldrich

Anti-SIL1 antibody produced in rabbit

affinity isolated antibody

Sinónimos:

Anti-BAP, Anti-MSS, Anti-SIL1 homolog, endoplasmic reticulum chaperone (S. cerevisiae), Anti-ULG5

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

49 kDa

species reactivity

human, guinea pig, bovine, rabbit, rat, horse

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIL1(64374)

Immunogen

Synthetic peptide directed towards the N terminal region of human SIL1

Application

Anti-SIL1 antibody produced in rabbit is suitable for western blotting at a concentration of 0.25μg/ml and for immunohistochemistry of paraffin-embedded tissue sections at a concentration of 4-8μg/ml.

Biochem/physiol Actions

SIL1 nucleotide exchange factor is an N-linked glycoprotein present in the membrane of endoplasmic reticulum. In coordination with HSPA5, SIL1 regulates proper folding of newly synthesized of proteins and degrades proteins that fail to mature properly. SIL1 is also regulated by glucose and its activity is essential for glucose-stimulated insulin secretion by the pancreatic beta cells. Mutations in SIL1 cause cerebellar ataxia, chronic myopathy, cataracts, delayed motor development and intellectual disability, collectively known as Marinesco-Sjögren syndrome.

Sequence

Synthetic peptide located within the following region: KETKAEEELDAEVLEVFHPTHEWQALQPGQAVPAGSHVRLNLQTGEREAK

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Kyung Tae Chung et al.
The Journal of biological chemistry, 277(49), 47557-47563 (2002-10-03)
We identified a mammalian BiP-associated protein, BAP, using a yeast two-hybrid screen that shared low homology with yeast Sls1p/Sil1p and mammalian HspBP1, both of which regulate the ATPase activity of their Hsp70 partner. BAP encoded an approximately 54-kDa protein with
Arne A Ittner et al.
Diabetologia, 57(7), 1410-1419 (2014-04-16)
Regulation of insulin secretion along the secretory pathway is incompletely understood. We addressed the expression of SIL1, a nucleotide exchange factor for the endoplasmic reticulum (ER) chaperone glucose-regulated protein 78 kD (GRP78), in pancreatic beta cells and investigated whether or not
Michael Krieger et al.
Brain : a journal of neurology, 136(Pt 12), 3634-3644 (2013-11-02)
Marinesco-Sjögren syndrome is a rare autosomal recessive multisystem disorder featuring cerebellar ataxia, early-onset cataracts, chronic myopathy, variable intellectual disability and delayed motor development. More recently, mutations in the SIL1 gene, which encodes an endoplasmic reticulum resident co-chaperone, were identified as
Yutaka Inaguma et al.
EMBO molecular medicine, 6(3), 414-429 (2014-01-30)
Marinesco-Sjögren syndrome (MSS) is a rare autosomal recessively inherited disorder with mental retardation (MR). Recently, mutations in the SIL1 gene, encoding a co-chaperone which regulates the chaperone HSPA5, were identified as a major cause of MSS. We here examined the

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