Recombinant Human Calcium-Binding And Coiled-Coil Domain-Containing Protein 2 (CALCOCO2) Protein (His)

Name: Recombinant Human Calcium-Binding And Coiled-Coil Domain-Containing Protein 2 (CALCOCO2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07221P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Calcium-Binding And Coiled-Coil Domain-Containing Protein 2 (CALCOCO2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13137
Target Symbol	CALCOCO2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPICKADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFCHSL
Expression Range	1-446aa
Protein Length	Full Length
Mol. Weight	58.3 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation. Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C. May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion.
Subcellular Location	Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein.
Protein Families	CALCOCO family
Database References	HGNC: 29912 OMIM: 604587 KEGG: hsa:10241 STRING: 9606.ENSP00000258947 UniGene: Hs.514920
Tissue Specificity	Expressed in all tissues tested with highest expression in skeletal muscle and lowest in brain.

Gene Functions References

Backfolding of MVI regulates its ability to bind DNA and that a putative transcription co-activator NDP52 relieves the auto-inhibition of MVI to enable DNA binding. Additionally, we show that the MVI-NDP52 complex binds RNAPII, which is critical for transcription, and that depletion of NDP52 or MVI reduces steady-state mRNA levels. PMID: 29187741
findings reveal a negative feedback loop of RLR signaling generated by Tetherin-MARCH8-MAVS-NDP52 axis and provide insights into a better understanding of the crosstalk between selective autophagy and optimal deactivation of type I IFN signaling. PMID: 28965816
The authors propose that Rab35-GTP is a critical regulator of autophagy through recruiting autophagy receptor NDP52. PMID: 28848034
The authors identify calcium-binding and coiled-coil domain 2 (CALCOCO2, also known as NDP52) as a binding partner of influenza A virus PB1-F2. PMID: 28613140
Presence of the NDP52 rs2303015 minor variant increases the risk for spontaneous bacterial peritonitis in patients with alcoholic cirrhosis. PMID: 26493630
insight into how CALCOCO2 targets ubiquitin-decorated pathogens for autophagic degradations PMID: 26506893
control retrotransposon insertion in the genome PMID: 25366815
These data show that NDP52 promotes the maturation of autophagosomes via its interaction with LC3A, LC3B, and/or GABARAPL2 through a distinct LC3-interacting region, and with MYOSIN VI. PMID: 25771791
data support a model in which non-ND10 resident Sp100 acts as a negative regulator of polycomb repressive complex-2 (PRC2) recruitment, and suggest that KSHV may actively escape ND10 silencing mechanisms to promote establishment of latent chromatin. PMID: 25033267
the role of ORF75 in the antagonization of ND10-mediated intrinsic immunity PMID: 24453968
Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules PMID: 23511477
The missense SNP rs2303015 (Val248Ala) in the NDP52 was associated with Crohn's disease. PMID: 23624108
Data indicate that the binding site in galectin-8 is essential for the recruitment of the autophagy receptor NDP52 to cytosol-exposed Salmonella Typhimurium. PMID: 23386746
Autophagy of Tax1bp1/Ndp52 promotes non-canonical NF-kappaB signalling. PMID: 23209807
Data show that the selectivity of the autophagy receptor NDP52 for LC3C is crucial for innate immunity since cells lacking either protein cannot protect their PMID: 23022382
Data show that the miRNA-processing enzyme, DICER and the main miRNA effector, AGO2, are targeted for degradation as miRNA-free entities PMID: 23143396
a selective autophagic mechanism mediated by NDP52 that works downstream of TRIF-TRAF6. PMID: 21964925
p62 and NDP52 act cooperatively to drive efficient antibacterial autophagy by targeting the protein complexes they coordinate to distinct microdomains associated with bacteria PMID: 21079414
p62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathways. PMID: 21646350
ND10 and ND10 components might be important defensive factors against the CMV cross-species infection PMID: 21552525
interacts with ICP4 regulatory protein of HSV-1 during early stage of infection PMID: 14747555
NDP52 was identified as a myosin VI binding protein; results suggest that myosin VI-T6BP-NDP52 complexes may play a role in coordinating cytokine signalling and membrane transport pathways with actin filament organisation and cell adhesion PMID: 17635994
NDP52 recognizes ubiquitin-coated Salmonella enterica and recruits TBK1. PMID: 19820708

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.