Cat: IPD-X29240

Recombinant Pig Calreticulin/CALR Protein (P. pastoris),His

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Analytical Data

  • Gene name

    Calreticulin/CALR

  • 简介

    Calreticulin (CALR) is an essential calcium-binding chaperone involved in ER functions. It interacts with glycoproteins, facilitates NR3C1 nuclear export, regulates maternal gene expression, and aids in oocyte maturation. CALR is released during oocyte activation and prevents polyspermy. It forms an EIF2 complex with CELF1/CUGBP1, CALR3, EIF2S1, EIF2S2, HSP90B1, and HSPA5 and interacts with PDIA3/ERp57, SPACA9, TRIM21, PPIB, PDIA5, and CLCC1. Calreticulin/CALR Protein, Pig (P.pastoris, His) is the recombinant pig-derived Calreticulin/CALR protein, expressed by P. pastoris , with N-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CALRCalreticulin; CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP

  • Species

    Pig

  • Source

    P. pastoris

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P28491

  • Expression Region

    E18-L417

  • AA Sequence

    EPTIYFKEQFLDGDGWTDRWIESKHKPDFGRFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPDGLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAVKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDSNIYAYENFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEEKKRKEEEEVDKEDEEDKDEDEEEEDEKEEEEEEDAAAGQAKDEL

  • Protein Length

    Full Length of Mature Protein

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

Calreticulin (CALR) is a multifunctional protein that plays a crucial role in calcium homeostasis, protein folding, and quality control in the endoplasmic reticulum (ER). It is involved in various cellular processes, including immune response and gene regulation. Recent studies have highlighted the significance of CALR mutations in hematological malignancies, particularly in myeloproliferative neoplasms (MPNs). These mutations often result in a type of calreticulin variant that interacts with the thrombopoietin receptor, leading to constitutive signaling and increased cell proliferation. As a result, CALR has emerged as a potential biomarker for the diagnosis and prognostication of MPNs. Research into recombinant CALR proteins has gained momentum, as these proteins are utilized to explore the functional consequences of CALR mutations and their impact on cell signaling pathways. Additionally, CALR's role in immune modulation has spurred interest in its potential therapeutic implications, particularly in cancer immunotherapy. By developing recombinant CALR proteins, scientists aim to dissect the mechanistic pathways influenced by CALR mutations, paving the way for targeted therapies and improved diagnostic tools. Overall, the study of CALR and its recombinant proteins represents a promising frontier in understanding disease mechanisms and developing innovative therapeutic strategies.

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