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SAB4200339

Sigma-Aldrich

Anti-XTP3-B antibody, Mouse monoclonal

clone XTP3-10, purified from hybridoma cell culture

Synonym(s):

Anti-C2orf30, Anti-ER lectin, Anti-ERLEC1, Anti-Endoplasmic reticulum lectin 1, Anti-Erlectin, Anti-XTP3-transactivated gene B protein, Anti-XTP3-transactivated protein, Anti-XTP3TPB

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

XTP3-10, monoclonal

form

buffered aqueous solution

mol wt

antigen ~54 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): suitable
western blot: 2-5 μg/mL using whole extracts of HEK-293T cells over-expressing human XTP3-B.

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ERLEC1(27248)

General description

Monoclonal Anti-XTP3-B (mouse IgG2b isotype) is derived from the hybridoma XTP3-10 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide. XTP3-transactivated gene B precursor (XTP3-B) belongs to the mannose-6-phosphate receptor homology (MRH) domain family, which comprises two MRH domains in its sequence. It is a luminal resident protein found in the endoplasmic reticulum. The XTP3-B gene is located at human chromosome 2p16.2.

Specificity

Monoclonal Anti-XTP3-B recognizes human XTP3-B.

Immunogen

synthetic peptide corresponding to an internal region of human XTP3-B, conjugated to KLH. The corresponding sequence differs by one amino acid in mouse and rat.

Application

Monoclonal Anti-XTP3-B antibody produced in mouse may be used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

XTP3-transactivated gene B precursor (XTP3-B) is implicated in endoplasmic reticulum (ER) quality control. It plays a role in ER-associated protein degradation (ERAD) selection and targeting processes. Human XTP3-B is linked with the suppressor of lin-12-like protein 1/ hydroxymethylglutaryl reductase degradation protein 1 (SEL1L/HRD1) ubiquitin ligase complex in the ER membrane and with the ER chaperone binding immunoglobulin protein (BiP) to form an ER quality control scaffold complex. This large complex, which also comprises the osteosarcoma 9 (OS-9) ER lectin, regulates the recognition and sorting of misfolded glycoproteins and non-glycosylated proteins before retrotranslocation.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8°C for up to one month. For extended storage, freeze at -20oC in working aliquots. Repeated freezing and thawing,or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

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

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Cristina-Maria Cruciat et al.
The Journal of biological chemistry, 281(18), 12986-12993 (2006-03-15)
Kremen1 and 2 (Krm1/2) are coreceptors for Dickkopf1 (Dkk1), an antagonist of Wnt/beta-catenin signaling, and play a role in head induction during early Xenopus development. In a proteomic approach we identified Erlectin, a novel protein that interacts with Krm2. Erlectin
Human XTP3-B forms an ER quality-control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
Hosokawa N, et al.
The Journal of Biological Chemistry, 283(30), 20914-20924 (2008)
Sweet bays of ERAD
Tamura T, et al.
Trends in Biochemical Sciences, 33(7), 298-300 (2008)
John C Christianson et al.
Nature cell biology, 10(3), 272-282 (2008-02-12)
Terminally misfolded or unassembled proteins in the early secretory pathway are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). How substrates of this pathway are recognized within the ER and delivered to the cytoplasmic ubiquitin-conjugating machinery

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