Human Recombinant COX4NB protein, His Tag (V2LY-0526-LY3346)

Name: Human Recombinant COX4NB protein, His Tag
SKU: V2LY-0526-LY3346
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

E. coli

Protein Species

Human

Tag

His Tag

Protein Construction

This product is Human Recombinant COX4NB protein, His Tag consist of Amino Acid: 1-210 and predicts a molecular mass of 25.6 kDa.

Molecule Mass

25.6 kDa

Sequence

Amino Acid: 1-210

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity

>95% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile Tris, NaCl, DTT

Preservative

None

Storage

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

More Infomation

Target

Full Name

ER Membrane Protein Complex Subunit 8

Research Area

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176, PubMed:32439656).

Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231).

Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151).

It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231).

By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835).

By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).

Biological Process

Protein insertion into ER membrane by stop-transfer membrane-anchor sequence Source: UniProtKB
Tail-anchored membrane protein insertion into ER membrane Source: UniProtKB

Cellular Location

Endoplasmic reticulum membrane

Iyer, A., Niemann, M., Serricchio, M., Dewar, C. E., Oeljeklaus, S., Farine, L., ... & Bütikofer, P. (2022). The endoplasmic reticulum membrane protein complex localizes to the mitochondrial-endoplasmic reticulum interface and its subunits modulate phospholipid biosynthesis in Trypanosoma brucei. PLoS pathogens, 18(5), e1009717.

Guna, A., Hazu, M., Tomaleri, G. P., & Voorhees, R. M. (2022). A TAle of Two Pathways: Tail-Anchored Protein Insertion at the Endoplasmic Reticulum. Cold Spring Harbor Perspectives in Biology, a041252.

Bai, L., & Li, H. (2022). Cryo‐EM structures of the endoplasmic reticulum membrane complex. The FEBS Journal, 289(1), 102-112.

Alvira, S., Corey, R. A., Collinson, I., & Römisch, K. (2021). Membrane protein biogenesis by the EMC. The EMBO Journal, 40(2), e107407.

Yang, M., Li, S., Liu, W., Li, X., He, Y., Yang, Y., ... & Zhu, X. (2021). The ER membrane protein complex subunit Emc3 controls angiogenesis via the FZD4/WNT signaling axis. Science China Life Sciences, 64(11), 1868-1883.

Pleiner, T., Tomaleri, G. P., Januszyk, K., Inglis, A. J., Hazu, M., & Voorhees, R. M. (2020). Structural basis for membrane insertion by the human ER membrane protein complex. Science, 369(6502), 433-436.

Pleiner, T., Januszyk, K., Tomaleri, G. P., Oania, R. S., Hazu, M., Sweredoski, M. J., ... & Voorhees, R. M. (2020). Regulated assembly of the ER membrane protein complex. bioRxiv.

Volkmar, N., Thezenas, M. L., Louie, S. M., Juszkiewicz, S., Nomura, D. K., Hegde, R. S., ... & Christianson, J. C. (2019). The ER membrane protein complex promotes biogenesis of sterol-related enzymes maintaining cholesterol homeostasis. Journal of Cell Science, 132(2), jcs223453.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
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Isotype control

For research use only. Not intended for any clinical use.

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