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Description:

B-Cell Leukemia/Lymphoma XL Mouse Recombinant

BclXL, Bcl-X(L), Bcl-XL.

Product # :

PRO-1362

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Description

Bcl-XL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids, having an MW of 23.7kDa.The Bcl-XL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Bcl-XL Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.
Synonyms
BclXL, Bcl-X(L), Bcl-XL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bcl-XL although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-XL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Bcl-XL in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-28B Mouse Recombinant

Interferon lambda-3, IFN-lambda-3, Interleukin-28B, IL-28B, Ifnl3, Il28, Il28b.

Product # :

CYT-732

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Description

IL-28B Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.6kDa.The IL28B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL28B protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 30 ng/ml, corresponding to a specific activity of > 3.3 × 10⁴ IU/mg.

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Introduction
IL-28B is a cytokine remotely related to type I interferons and the IL-10 family. Interleukin-28B, interleukin 28A (IL28A), and interleukin 29 (IL29) are 3 closely related cytokine genes which form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by these 3 genes can be induced by viral infection. All 3 cytokines interact with a heterodimeric class II cytokine receptor which consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha (IL28RA).
Synonyms
Interferon lambda-3, IFN-lambda-3, Interleukin-28B, IL-28B, Ifnl3, Il28, Il28b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-28B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL28B should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-28B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKGAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENINDS ALTTILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFQLL LRDLKCVASG DQCV.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-3 Receptor Subunit Alpha Mouse Recombinant

Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

Product # :

CYT-1210

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Description

IL3RA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-331 a.a.) and fused to a 231 a.a. Human IgG His Tag at C-terminus containing a total of 554 amino acids and having a molecular mass of 61.5 kDa.

Source

Sf9, Baculovirus cells.

Formulation

IL3RA protein solution (0.25mg/ml) contains 20mM Tris-HCL, 30% glycerol & 0.1M NaCl (pH-8).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH
Background
What is the molecular weight/Mw of IL 3 RA MOUSE Protein?
IL 3 RA MOUSE Protein has a total Mw of 61.5kDa.

What is the source or expression system of IL 3 RA MOUSE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 3 RA MOUSE Protein?
IL 3 RA MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RA MOUSE Protein?
The biological functionality of IL 3 RA MOUSE Protein will be determined in the future.

What is the amino acid sequence of IL 3 RA MOUSE Protein?
SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

What applications can IL 3 RA MOUSE Protein be used in?
IL 3 RA MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RA MOUSE Protein?
The endotoxin level is minimal, IL 3 RA MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RA MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 RA MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Influenza-B Virus Jilin 20/2003 Recombinant

Product # :

IHA-021

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Description

Recombinant Full-Length B/Jilin/20/2003 is glycosylated with N-linked sugars, produced using baculovirus vectors in insect cells.

Source

Baculovirus Insect Cells.

Formulation

The Recombinant B/Jilin/20/2003 solution contains 10mM Sodium phosphate, pH 7.4 and 150mM Sodium Cloride.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Influenza-B virus is a genus in the virusfamily Orthomyxoviridae. The only species in this genus is called "Influenza B virus". Influenza B virus only infects humansand seals. This limited host range is apparently in contrast with those caused by the similar Influenza virus Aas both mutate by both genetic drift and reassortment. Influenza-B virus evolves slower than A viruses and faster than C viruses. Influenza-B virus mutates at a rate 2-3 times lower than type A. However, influenza B mutates enough that lasting immunity is not possible. The Influenza B virus capsidis enveloped while its virionconsists of a matrix protein + envelope + nucleoprotein complex + nucleocapsid, and a polymerasecomplex. Influenza B is sometimes spherical and sometimes filamentous. Its 500 or so surface projections are made of hemagglutinin and neuraminidase.
The Influenza B virus is 14648 nucleotideslong and consists of eight segments of linear negative-sense, single-stranded RNA. The multipartite genome is encapsidated, each segment in a separate nucleocapsid, and the nucleocapsids are surrounded by one envelope.
Physical Appearance
Sterile Filtered colorless solution.
Stability
B/Jilin/20/2003 Recombinant should be stored at 4°C.
Immunological Activity
Western-Blot 0.1µg -1µg per strip, ELISA 1µg/Well.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

H3N2 Influenza A- Virus Hong Kong 4801/2014 Recombinant

Product # :

IHA-043

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Description

Recombinant Full-Length H3N2 Hong Kong 4801/2014 is glycosylated with N-linked sugars, produced using baculovirus vectors in insect cells.

Source

Baculovirus Insect Cells.

Formulation

The Recombinant H3N2 A/ Hong Kong 4801/2014 solution contains 10mM Sodium phosphate, pH 7.4,150mM NaCl and 0.005% Tween-20.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2 by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.
Physical Appearance
Sterile Filtered colorless solution.
Stability
H3N2 A/ Hong Kong 4801/2014 recombinant should be stored at 4°C. Do not freeze!

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Serpin Peptidase Inhibitor, Clade F Member 2 Mouse Recombinant

Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.

Product # :

PRO-2240

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Description

SERPINF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 470 amino acids (28-491 a.a.) and having a molecular mass of 52.9kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). SERPINF2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SERPINF2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.
Synonyms
Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
VDLPGQQPVS EQAQQKLPLP ALFKLDNQDF GDHATLKRSP GHCKSVPTAE ETRRLAQAMM AFTTDLFSLV AQTSTSSNLV LSPLSVALAL SHLALGAQNQ TLHSLHRVLH MNTGSCLPHL LSHFYQNLGP GTIRLAARIY LQKGFPIKDD FLEQSERLFG AKPVKLTGKQ EEDLANINQW VKEATEGKIE DFLSELPDST VLLLLNAIHF HGFWRTKFDP SLTQKDFFHL DERFTVSVDM MHAVSYPLRW FLLEQPEIQV AHFPFKNNMS FVVVMPTYFE WNVSEVLANL TWDTLYHPSL QERPTKVWLP KLHLQQQLDL VATLSQLGLQ ELFQGPDLRG ISEQNLVVSS VQHQSTMELS EAGVEAAAAT SVAMNRMSLS SFTVNRPFLF FIMEDTIGVP LFVGSVRNPN PSALPQLQEQ RDSPDNRLIG QNDKADFHGG KTFGPDLKLA PRMEEDYPQF SSPKHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

B-Cell Leukemia/Lymphoma 2, (1-206 a.a.) Human Recombinant

Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

Product # :

PRO-630

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Description

Bcl-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-206. The wild type Bcl-2 is missing 12 amino acids from C-terminus. C-terminus is fused to His-Tag. C-terminus his-tag, mimics the deleted C-terminus membrane domain thus maintaining its biological activity. Bcl-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Suspend Bcl-2 in 100ul of 0.5M Acetic acid, over night at 4°C. Dilute 10 fold into selected buffer system. BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

BCL2 Like 11 Human Recombinant

Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.

Product # :

PRO-1171

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Description

BCL2L11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-138 a.a) and having a molecular mass of 18.5kDa.BCL2L11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

BCL2L11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 2M Urea, 20% glycerol, 5mM DTT and 300mM NaCl.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Bcl-2-like protein 11 (BCL2L11) is a member of the Bcl-2 family and contains a Bcl-2 homology domain 3 (BH3). BCL2L11 expression can be stimulated by nerve growth factor (NGF), in addition to the forkhead transcription factor (FKHR-L1) which proposes a role of the BCL2L11 gene in neuronal and lymphocyte apoptosis. BCL2L11 interacts with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and acts as an apoptotic activator. BimEL, BimL and BimS are the main isoforms which are ubiquitously expressed with a tissue-specific variation. The Isoform Bim-gamma, on the other hand, is most abundantly expressed in the small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney.
Synonyms
Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAKQPS DVSSECDREG RQLQPAERPP QLRPGAPTSL QTEPQDRSPA PMSCDKSTQT PSPPCQAFNH YLSAMASMRQ AEPADMRPEI WIAQELRRIG DEFNAYYARR VFLNNYQAAE DHPRMVILRL LRYIVRLVWR MH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-20 Mouse Recombinant

IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.

Product # :

CYT-379

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Description

Interleukin-20 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a total molecular mass of 17,584 Dalton. The IL-20 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity was determined by measuring the dose dependent activation of STAT3 in human epidermal keratinocytes (HEK2a cells). Significant STAT3 activation is observed with >100ng/mL of Interleukin-20 recombinant mouse, corresponding to a specific activity of 10,000 units/mg of Interleukin-20 recombinant mouse.

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Introduction
IL20 is a cytokine structurally related to interleukin 10 (IL10). IL20 cytokine has been shown to transduce its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. A specific receptor for this cytokine is found to be expressed in skin and upregulated dramatically in psoriatic skin, suggesting a role for this protein in epidermal function and psoriasis.
Synonyms
IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL20 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Lys-Thr-Leu.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.552 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-20 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thioredoxin-Like 4A Human Recombinant

Thioredoxin-like 4A, Spliceosomal U5 snRNP-specific 15 kDa protein, DIM1 protein homolog, HsT161, TXNL4, DIB1, U5-15kD.

Product # :

PRO-1100

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Description

TXNL4A Human Recombinant produced in E. coli is a single polypeptide chain containing 166 amino acids (1-142) and having a molecular mass of 19.3kDa.TXNL4A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TXNL4A solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 200mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
TXNL4A is a member of the Dim protein family and has a vital part in pre-mRNA splicing. As a result of a failure to express early zygotic transcripts, deletion of the gene encoding TXNL4A in Schizosaccharomyces pombe results in embryonal lethality during gastrulation. Restricted to the nucleus, TXNL4A cooperates with hnRNP F, hnRNP H2, Cas-L and PQBP-1 to influence gene expression.
Synonyms
Thioredoxin-like 4A, Spliceosomal U5 snRNP-specific 15 kDa protein, DIM1 protein homolog, HsT161, TXNL4, DIB1, U5-15kD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSYMLP HLHNGWQVDQ AILSEEDRVV VIRFGHDWDP TCMKMDEVLY SIAEKVKNFA VIYLVDITEV PDFNKMYELY DPCTVMFFFR NKHIMIDLGT GNNNKINWAM EDKQEMVDII ETVYRGARKG RGLVVSPKDY STKYRY

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

DEAD Box Protein 39A Human Recombinant

DEAD (Asp-Glu-Ala-Asp) box polypeptide 39A, BAT1, BAT1L, DDX39, DDXL, URH49, ATP-dependent RNA helicase DDX39A, DEAD box protein 39, Nuclear RNA helicase URH49, DDX39A.

Product # :

PRO-1990

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Description

DDX39A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31kDa. DDX39A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DDX39A protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
DDX39A which is a part of the DEAD box protein family is characterized by the conserved motif Asp-Glu-Ala-Asp. This pattern is implicated in a various cellular processes involving alteration of RNA secondary structure, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Several members of the DEAD box protein family are taking part in embryogenesis, spermatogenesis, and cellular growth and division.
Synonyms
DEAD (Asp-Glu-Ala-Asp) box polypeptide 39A, BAT1, BAT1L, DDX39, DDXL, URH49, ATP-dependent RNA helicase DDX39A, DEAD box protein 39, Nuclear RNA helicase URH49, DDX39A.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMAEQD VENDLLDYDE EEEPQAPQES TPAPPKKDIK GSYVSIHSSG FRDFLLKPEL LRAIVDCGFE HPSEVQHECI PQAILGMDVL CQAKSGMGKT AVFVLATLQQ IEPVNGQVTV LVMCHTRELA FQISKEYERF SKYMPSVKVS VFFGGLSIKK DEEVLKKNCP HVVVGTPGRI LALVRNRSFS LKNVKHFVLD ECDKMLEQLD MRRDVQEIFR LTPHEKQCMM FSATLSKDIR PVCRKFMQDP MEVF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

BCL2-Like 1 Recombinant Mouse

Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.

Product # :

PRO-2239

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Description

BCL2L1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a) and having a molecular mass of 25.8kDa. BCL2L1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BCL2L1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
BCL2-Like 1 (BCL2L1) belongs to the BCL-2 protein family. BCL2L1 is found at the outer mitochondrial membrane controls outer mitochondrial membrane channel (VDAC) opening. In addition, BCL2L1 regulate s a switch between cell death modes during mitotic arrest.
Synonyms
Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSQSNRE LVVDFLSYKL SQKGYSWSQF SDVEENRTEA PEETEAERET PSAINGNPSW HLADSPAVNG ATGHSSSLDA REVIPMAAVK QALREAGDEF ELRYRRAFSD LTSQLHITPG TAYQSFEQVV NELFRDGVNW GRIVAFFSFG GALCVESVDK EMQVLVSRIA SWMATYLNDH LEPWIQENGG WDTFVDLYGN NAAAESRKGQ ER.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GroEL (HSP60) E.Coli Recombinant

CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.

Product # :

HSP-004

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Description

Recombinant GroEL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-548) and having a molecular mass of 57.3kDa. GroEL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The groEL protein contains 25mM Tris buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.
Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREIELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGIDKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDGTGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAVAKAGKPLLII AEDVEGEALA TAVVNTIRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTVISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDYDREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALIRVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNAATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

V-ral Simian Leukemia Viral Oncogene Homolog A Mouse Recombinant

Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.

Product # :

PRO-2497

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Description

RALA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a) and having a molecular mass of 25.7kDa. RALA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RALA protein solution (0.5mg/ml) 20mM Tris-Hcl buffer (pH8.5) containing 30% glycerol, 0.1M NaCl and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.
Synonyms
Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA DQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CTACK Mouse Recombinant (CCL27)

C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

Product # :

CHM-013

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

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Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
Synonyms
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CTACK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
Background
What is the molecular weight/Mw of CTACK MOUSE Protein?
CTACK MOUSE Protein has a total Mw of 10.9kDa.

What is the source or expression system of CTACK MOUSE Protein?
Escherichia Coli.

What is the Purity of CTACK MOUSE Protein?
CTACK MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CTACK MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CTACK MOUSE Protein?
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

What applications can CTACK MOUSE Protein be used in?
CTACK MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTACK MOUSE Protein?
The endotoxin level is minimal, CTACK MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CTACK MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CTACK MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)

Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

Product # :

CHM-320

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 1mg/ml solution containing no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
Background
What is the molecular weight/Mw of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein has a total Mw of 7.82kDa.

What is the source or expression system of MIP 1A MOUSE Protein?
Escherichia Coli.

What is the Purity of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of MIP 1A MOUSE Protein?
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of MIP 1A MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.

What applications can MIP 1A MOUSE Protein be used in?
MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for MIP 1A MOUSE Protein?
The endotoxin level is minimal, MIP 1A MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Coxsackie Virus And Adenovirus Receptor Human Recombinant

Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.

Product # :

PRO-1548

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Description

CXADR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (20-237) and having a molecular mass of 26.0kDa.CXADR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXADR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CXADR is a component of the epithelial apical junction complex which operates as an homophilic cell adhesion molecule and is crucial for tight junction integrity. CXADR also takes part in transepithelial relocation of leukocytes through adhesive interactions with AMICA1/JAML a transmembrane protein of the plasma membrane of leukocytes. A number of transcript variants encoding different isoforms were identified for this gene. Pseudogenes of this gene were located on chromosomes 15, 18, and 21.
Synonyms
Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLSITTPE EMIEKAKGET AYLPCKFTLS PEDQGPLDIE WLISPADNQK VDQVIILYSG DKIYDDYYPD LKGRVHFTSN DLKSGDASIN VTNLQLSDIG TYQCKVKKAP GVANKKIHLV VLVKPSGARC YVDGSEEIGS DFKIKCEPKE GSLPLQYEWQ KLSDSQKMPT SWLAEMTSSV ISVKNASSEY SGTYSCTVRN RVGSDQCLLR LNVVPPSNKA G.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

I-TAC Human Recombinant (CXCL11), His Tag

Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

Product # :

CHM-232

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Description

I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
Synonyms
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.
Background
What is the molecular weight/Mw of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein has a total Mw of 10.6kDa.

What is the source or expression system of CXCL11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL11 HUMAN, HIS Protein?
The biological functionality of CXCL11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.

What applications can CXCL11 HUMAN, HIS Protein be used in?
CXCL11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL11 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL11 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL11 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL11 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interferon-Omega 1 Human Recombinant, HEK

IFN omega-1, IFN alpha-II-1, IFNW1.

Product # :

CYT-1225

Price :

Quantity :

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Description

IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.

What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.

What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 HUMAN, HEK Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant (CXCL5)

C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

Product # :

CHM-365

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Quantity :

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Description

Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 9.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM sodium phosphate buffer, pH 7.4 & 150mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
Synonyms
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.
Background
What is the molecular weight/Mw of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein has a total Mw of 9.8kDa.

What is the source or expression system of CXCL5 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL5 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CXCL5 MOUSE Protein?
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.

What applications can CXCL5 MOUSE Protein be used in?
CXCL5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL5 MOUSE Protein?
The endotoxin level is minimal, CXCL5 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL5 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL5 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GREM2 Human Recombinant

CKTSF1B2, DAND3, PRDC, Gremlin-2, Cysteine knot superfamily 1, BMP antagonist 2, DAN domain family member 3, Protein related to DAN and cerberus, GREM2.

Product # :

PRO-1428

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Shipping Method :

Shipped with Ice Packs

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Description

GREM2 Human Recombinant produced in E. coli is a single polypeptide chain containing 170 amino acids (22-168) and having a molecular mass of 19kDa. GREM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GREM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
GREM2 which is a member of the BMP (bone morphogenic protein) antagonist family takes part in regulating organogenesis, body patterning, and tissue differentiation. GREM2 is an antagonist of BMP and like BMPs, BMP antagonists contain cystine knots and typically form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, is characterized by a C-terminal cystine knot with an 8-membered ring.
Synonyms
CKTSF1B2, DAND3, PRDC, Gremlin-2, Cysteine knot superfamily 1, BMP antagonist 2, DAN domain family member 3, Protein related to DAN and cerberus, GREM2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRKNRPAG AIPSPYKDGS SNNSERWQHQ IKEVLASSQE ALVVTERKYL KSDWCKTQPL RQTVSEEGCR SRTILNRFCY GQCNSFYIPR HVKKEEESFQ SCAFCKPQRV TSVLVELECP GLDPPFRLKK IQKVKQCRCM SVNLSDSDKQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GRO-Alpha Human Recombinant (CXCL1)

Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

Product # :

CHM-329

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Shipped at Room temp

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sds-page
Citations

Description

GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

sds-page

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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GRO-Gamma Mouse Recombinant (CXCL3), His Tag

C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

Product # :

CHM-283

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Shipped with Ice Packs

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Description

GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
Synonyms
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
Background
What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

What is the source or expression system of CXCL3 MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

What applications can CXCL3 MOUSE, HIS Protein be used in?
CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL3 MOUSE, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL3 MOUSE, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CD40 Human Recombinant, HEK

CD40 Molecule, TNF Receptor Superfamily Member 5, TNFRSF5, Tumor Necrosis Factor Receptor Superfamily, Member 5, Bp50, B-Cell Surface Antigen CD40, CD40L Receptor, CDW40, B Cell Surface Antigen CD40, B Cell-Associated Molecule, CD40 Antigen (TNF Receptor Superfamily Member 5), CD40 Type II Isoform, Nerve Growth Factor Receptor-Related B-Lymphocyte Activation Molecule, p50, Tumor Necrosis Factor Receptor Superfamily Member 5, CDw40, CD40 Antigen

Product # :

PRO-2719

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Description

CD40 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 412 amino acids (21-193 a.a.) and having a molecular mass of 46.1kDa.CD40 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

CD40 protein solution (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CD40 belongs to the TNF-receptor super family. CD40 has been found to be vital in mediating a wide range of immune and inflammatory responses including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. AT-hook transcription factor AKNA is accounted to coordinately regulate the expression of CD40 and its ligand, which is significant for homotypic cell interactions. Adaptor protein TNFR2 interacts with CD40 and functions as a mediator of the signal transduction. The interaction of CD40 and its ligand is found to be essential for amyloid-beta-induced microglial activation, and therefore is considered to be an early event in Alzheimer disease pathogenesis.
Synonyms
CD40 Molecule, TNF Receptor Superfamily Member 5, TNFRSF5, Tumor Necrosis Factor Receptor Superfamily, Member 5, Bp50, B-Cell Surface Antigen CD40, CD40L Receptor, CDW40, B Cell Surface Antigen CD40, B Cell-Associated Molecule, CD40 Antigen (TNF Receptor Superfamily Member 5), CD40 Type II Isoform, Nerve Growth Factor Receptor-Related B-Lymphocyte Activation Molecule, p50, Tumor Necrosis Factor Receptor Superfamily Member 5, CDw40, CD40 Antigen
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
EPPTACREKQ YLINSQCCSL CQPGQKLVSD CTEFTETECL PCGESEFLDT WNRETHCHQH KYCDPNLGLR VQQKGTSETD TICTCEEGWH CTSEACESCV LHRSCSPGFG VKQIATGVSD TICEPCPVGF FSNVSSAFEK CHPWTSCETK DLVVQQAGTN KTDVVCGPQD RLRLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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