Search: 1000 results found for "influenza"

Description:

Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)

Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

Product # :

CHM-230

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM 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 T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
Background
What is the molecular weight/Mw of CCL15 HUMAN Protein?
CCL15 HUMAN Protein has a total Mw of 10.1kDa.

What is the source or expression system of CCL15 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL15 HUMAN Protein?
CCL15 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL15 HUMAN Protein?
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL15 HUMAN Protein?
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.

What applications can CCL15 HUMAN Protein be used in?
CCL15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL15 HUMAN Protein?
The endotoxin level is minimal, CCL15 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL15 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 CCL15 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:

HIV-1 Tat Interactive Protein 2 Human Recombinant

TIP30, CC3, SDR44U1, HTATIP2, EC=1.1.1.-, HIV-1 TAT-interactive protein 2, FLJ26963.

Product # :

ENZ-546

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

HTATIP2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-242 a.a.) and having a molecular mass of 29.3 kDa. The HTATIP2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HTATIP2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
HTATIP2 is part of the short-chain dehydrogenases/reductases (SDR) family which acts as a tumor suppressor in metabolic suppression, inhibition of angiogenesis and induces the expression of apoptosis related genes Bad and Siva. HTATIP2 cooperates with the activation domain of HIV-1 TAT and enhances its transcription by phosphorylating RNA polymerase II (Pol II). Defects in HTATIP2 are related with hepatocellular carcinomas and apoptotic resistant tumor cells, implicating a probable use for HTATIP2 in antitumor therapy.
Synonyms
TIP30, CC3, SDR44U1, HTATIP2, EC=1.1.1.-, HIV-1 TAT-interactive protein 2, FLJ26963.
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 MAETEALSKL REDFRMQNKS VFILGASGET GRVLLKEILE QGLFSKVTLI GRRKLTFDEE AYKNVNQEVV DFEKLDDYAS AFQGHDVGFC CLGTTRGKAG AEGFVRVDRD YVLKSAELAK AGGCKHFNLL SSKGADKSSN FLYLQVKGEV EAKVEELKFD RYSVFRPGVL LCDRQESRPG EWLVRKFFGS LPDSWARGHS VPVVTVVRAM LNNVVRPRDK QMELLENKAI HDLGKAHGSL KP.

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-gamma Canine Recombinant, His Tag

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-1022

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IFNG Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids (24-166 a.a) and having a molecular mass of 19.3kDa. IFNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNG protein solution (0.5mg/ml) contains 20mM MES (pH6.0), 20% glycerol, 0.1M NaCl and 1mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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 MGSQAMFFKE IENLKEYFNA SNPDVSDGGS LFVDILKKWR EESDKTIIQS QIVSFYLKLF DNFKDNQIIQ RSMDTIKEDM LGKFLNSSTS KREDFLKLIQ IPVNDLQVQR KAINELIKVM NDLSPRSNLR KRKRSQNLFR GRRASK.
Background
What is the molecular weight/Mw of IFNG CANINE, HIS Protein?
IFNG CANINE, HIS Protein has a total Mw of 19.3kDa.

What is the source or expression system of IFNG CANINE, HIS Protein?
Escherichia Coli.

What is the Purity of IFNG CANINE, HIS Protein?
IFNG CANINE, HIS Protein is >95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of IFNG CANINE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSQAMFFKE IENLKEYFNA SNPDVSDGGS LFVDILKKWR EESDKTIIQS QIVSFYLKLF DNFKDNQIIQ RSMDTIKEDM LGKFLNSSTS KREDFLKLIQ IPVNDLQVQR KAINELIKVM NDLSPRSNLR KRKRSQNLFR GRRASK.

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

What is the endotoxin level for IFNG CANINE, HIS Protein?
The endotoxin level is minimal, IFNG CANINE, HIS 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:

Interleukin-3 Rhesus Macaque Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399

Product # :

CYT-156

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

IL 3 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a molecular mass of 14.0kDa.The IL 3 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human
TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

More Info

Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ
Background
What is the molecular weight/Mw of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein has a total Mw of 14kDa.

What is the source or expression system of IL 3 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of IL 3 RHESUS MACAQUE Protein?
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ.

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

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

Who supplies recombinant IL 3 RHESUS MACAQUE 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 RHESUS MACAQUE?
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:

Interleukin 13 Receptor, Alpha 2 Human Recombinant

CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

Product # :

CYT-757

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

IL13RA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (27-343 a.a.) and having a molecular mass of 39.5kDa.IL13RA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL13RA2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.
Synonyms
CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.
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 MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.
Background
What is the molecular weight/Mw of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein has a total Mw of 39.5kDa.

What is the source or expression system of IL13RA2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13RA2 HUMAN Protein?
The biological functionality of IL13RA2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL13RA2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.

What applications can IL13RA2 HUMAN Protein be used in?
IL13RA2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13RA2 HUMAN Protein?
The endotoxin level is minimal, IL13RA2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13RA2 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 IL13RA2 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:

Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag

C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

Product # :

CHM-032

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TECK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils.
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Physical Appearance
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 MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
Background
What is the molecular weight/Mw of CCL25 HUMAN, HIS Protein?
CCL25 HUMAN, HIS Protein has a total Mw of 16.8kDa.

What is the source or expression system of CCL25 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL25 HUMAN, HIS Protein?
CCL25 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL25 HUMAN, HIS Protein?
The biological functionality of CCL25 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL25 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.

What applications can CCL25 HUMAN, HIS Protein be used in?
CCL25 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL25 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL25 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL25 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 CCL25 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:

IP-10 Human Recombinant (CXCL10)

Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

Product # :

CHM-330

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

IP-10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa. The IP-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types in response to IFN. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 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 IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKA IKNLLKAVSKERSKRSP.
Background
What is the molecular weight/Mw of CXCL10 HUMAN Protein?
CXCL10 HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of CXCL10 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL10 HUMAN Protein?
CXCL10 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 HUMAN Protein?
The biological functionality of CXCL10 HUMAN Protein will be determined in the future.

What is the amino acid sequence of CXCL10 HUMAN Protein?
VPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKA IKNLLKAVSKERSKRSP.

What applications can CXCL10 HUMAN Protein be used in?
CXCL10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL10 HUMAN Protein?
The endotoxin level is minimal, CXCL10 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL10 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 CXCL10 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:

IFN Regulatory Factor-3 Human Recombinant

IRF-3, IRF3, IFN Regulatory Factor 3.

Product # :

CYT-292

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IRF-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (1-112) and having a molecular mass of 13 kDa.The IRF3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml in phosphate-buffered saline (PBS), pH 7.4.

Purity

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

More Info

Introduction
Members of the IFN regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates IFN-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn-alpha and ifn-beta promoters respectively. IRF-3 does not have any transcription activation domains.
Synonyms
IRF-3, IRF3, IFN Regulatory Factor 3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid IRF3 although stable at 10°C for 1 week, should be stored 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.
Amino Acid Sequence
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.
Background
What is the molecular weight/Mw of IRF3 HUMAN Protein?
IRF3 HUMAN Protein has a total Mw of 13kDa.

What is the source or expression system of IRF3 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF3 HUMAN Protein?
IRF3 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF3 HUMAN Protein?
The biological functionality of IRF3 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF3 HUMAN Protein?
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.

What applications can IRF3 HUMAN Protein be used in?
IRF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF3 HUMAN Protein?
The endotoxin level is minimal, IRF3 HUMAN 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:

HIV-2 gp32 Recombinant, HRP Labeled

Product # :

HIV-137

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

HIV-2 gp32 HRP Labeled recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32 having a Mw of 32kDa and fused to a beta-galactosidase at N-terminus.

Source

Escherichia Coli.

Formulation

0.01M Na2CO3, 10mM EDTA, 14mM beta-ME and 0.02% Sarcosyl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids.
Immunodeficiency develops more slowly with HIV-2.
HIV-2 is less infectious in the early stages of the virus than with HIV-1.
The infectiousness of HIV-2 increases as the virus progresses.
Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.
HIV-1 gp41 helical regions can form more stable 6-helix bundles than
HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition.
Physical Appearance
Sterile filtered colorless clear solution.
Stability
HIV-2 gp-32 although stable at room temperature for 3 weeks, should be stored at 4°C.

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-4 Human Recombinant, His Tag

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-483

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
SDS-PAGE
Citations

Description

Interleukin-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-4 His-Tag is supplied in 20mM Tris-HCl and10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

SDS-PAGE

More Info

Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Recombinant IL-4 (Interleukin-4) is a bioengineered version of a naturally occurring cytokine, which plays a crucial role in the immune system. IL-4 is primarily produced by activated T cells, mast cells, and basophils, and it is involved in the regulation of immune responses, including the differentiation of T helper cells, B cell activation, and the production of immunoglobulins.Recombinant IL-4 is synthesized using recombinant DNA technology, which involves inserting the gene encoding IL-4 into a suitable expression system, such as bacteria, yeast, or mammalian cells. The host cells are then cultured, allowing them to produce the desired protein, which can be purified and used for various applications.One of the main functions of IL-4 is to promote the differentiation of naïve CD4+ T cells into T helper 2 (Th2) cells. Th2 cells are essential for coordinating immune responses against extracellular pathogens, such as parasites and allergens. They achieve this by secreting cytokines, including IL-4 itself, IL-5, and IL-13, which stimulate B cells to produce specific antibodies, eosinophils to combat parasites, and mast cells to release histamine and other inflammatory mediators.Recombinant IL-4 has been extensively studied for its potential therapeutic applications. It has been shown to have anti-inflammatory properties, making it a potential candidate for the treatment of autoimmune and inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and inflammatory bowel disease. Additionally, IL-4 has been found to inhibit the growth of certain cancer cells, suggesting that it may have potential as an anti-cancer agent.However, the use of recombinant IL-4 as a therapeutic agent is not without challenges. One of the main concerns is the potential for adverse effects due to its immunomodulatory properties. For example, excessive IL-4 activity can lead to the development of allergies and asthma, as it promotes the production

What is the molecular weight/Mw of IL 4 HUMAN, HIS Protein?
IL 4 HUMAN, HIS Protein has a total Mw of 17.2kDa.

What is the source or expression system of IL 4 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL 4 HUMAN, HIS Protein?
IL 4 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 HUMAN, HIS Protein?
The ED50 for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

What is the amino acid sequence of IL 4 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.

What applications can IL 4 HUMAN, HIS Protein be used in?
IL 4 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 HUMAN, HIS Protein?
The endotoxin level is minimal, IL 4 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 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 IL 4 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:

SARS-CoV Nucleocapsid (422a.a) Recombinant

Product # :

SARS-250

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

The Recombinant SARS-CoV Nucleocapsid Protein is manufactured with N-terminal fusion His Tag. The Recombinant SARS-CoV Nucleocapsid His-Tagged Fusion Protein is 47.8kDa containing 437 amino acid residues of the SARS-CoV Nucleocapsid protein and 16 additional amino acid residues – His Tag (underlined).

Source

Escherichia coli.

Formulation

Sterile filtered (0,4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH4.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MRGSHHHHHH GMASHMSDNG PQSNQRSAPR ITFGGPTDST DNNQNGGRNG ARPKQRRPQG LPNNTASWFT ALTQHGKEEL RFPRGQGVPI NTNSGPDDQI GYYRRATRRV RGGDGKMKEL SPRWYFYYLG TGPEASLPYG ANKEGIVWVA TEGALNTPKD HIGTRNPNNN AATVLQLPQG TTLPKGFYAE GSRGGSQASS RSSSRSRGNS RNSTPGSSRG NSPARMASGG GETALALLLL DRLNQLESKV SGKGQQQQGQ TVTKKSAAEA SKKPRQKRTA TKQYNVTQAF GRRGPEQTQG NFGDQDLIRQ GTDYKHWPQI AQFAPSASAF FGMSRIGMEV TPSGTWLTYH GAIKLDDKDP QFKDNVILLN KHIDAYKTFP PTEPKKDKKK KTDEAQPLPQ RQKKQPTVTL LPAADMDDFS RQLQNSMSGA SADSTQA.

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:

MIP-2 Viral Recombinant

MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.

Product # :

CHM-376

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

MIP-2 Viral Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 1mg/ml solution containing 20mM Phospahte Buffer, pH 7.4 % 0.15M NaCl.

Purity

Greater than 97.0% as determined by RP-HPLC & SDS-PAGE.

Biological Activity

Determined by the inhibitory effect on monocyte migration response to human MIP1A using a concentration range of 1µg-10µg/ml of viral MIP2 which will inhibit 25ng/ml of human MIP1A.

More Info

Introduction
Viral MIP-2 is closely related to MIP-1α, show amino acid sequence similarity of about 41%. At the amino acid sequence level, Viral MIP-1 and Viral MIP-2 share 48% similarity. Viral MIP-1 and Viral MIP-2 are more closely linked to one another phylogenetically than to other human chemokines, signifying that they have gene duplication within the virus rather than by two independent gene aquisitions. Viral MIP-2 binds to the CCR3 chemokine receptor through which eotaxin and other β chemokines activate eosinophils. Viral MIP-2 activates and chemoattract human eosinphils.
Synonyms
MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-2 Viral protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 CXCL2 Viral in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LGASWHRPDK CCLGYQKRPL PQVLLSSWYP TSQLCSKPGV IFLTKRGRQV
CADKSKDWVK KLMQQLPVTA.
Background
What is the molecular weight/Mw of VMIP-II Protein?
VMIP-II Protein has a total Mw of 7.9kDa.

What is the source or expression system of VMIP-II Protein?
Escherichia Coli.

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

What is the Biological Activity of VMIP-II Protein?
Determined by the inhibitory effect on monocyte migration response to human MIP1A using a concentration range of 1µg-10µg/ml of viral MIP2 which will inhibit 25ng/ml of human MIP1A.

What is the amino acid sequence of VMIP-II Protein?
LGASWHRPDK CCLGYQKRPL PQVLLSSWYP TSQLCSKPGV IFLTKRGRQV
CADKSKDWVK KLMQQLPVTA.

What applications can VMIP-II Protein be used in?
VMIP-II Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for VMIP-II Protein?
The endotoxin level is minimal, VMIP-II Protein was purified using conventional chromatography techniques.

Who supplies recombinant VMIP-II 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 VMIP-II?
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:

Lymphotactin (XCL1) Mouse Recombinant

XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

Product # :

CHM-037

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.Lymphotactin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, 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 a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells is < 100 ng/ml, corresponding to a specific activity of > 1.0 × 10⁴ IU/mg.

More Info

Introduction
XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.
Background
What is the molecular weight/Mw of LYMPHOTACTIN MOUSE Protein?
LYMPHOTACTIN MOUSE Protein has a total Mw of 10.1kDa.

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

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

What is the Biological Activity of LYMPHOTACTIN MOUSE Protein?
The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells is < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.

What is the amino acid sequence of LYMPHOTACTIN MOUSE Protein?
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.

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

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

Who supplies recombinant LYMPHOTACTIN 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 LYMPHOTACTIN 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:

Hepatitis B Virus x Recombinant

Product # :

HBV-273

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Hepatitis B Virus Protein X is a 17kDa protein containing 154 amino acid residues and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH4 and 5% trehalose.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Hepatitis B virus X protein (HBx) is a 17 kD transcriptional coactivator that plays a significant role in the regulation of genes involved in inflammation and cell survival. It regulates many transcription factors including nuclear factor kappa B (NF-kappaB) and plays a key role in hepatocarcinogenesis. rHBx facilitates the binding of cAMP response element binding protein (CREB) to its responsive element. rHBx stabilizes the cellular coactivator ASC-2 through direct protein-protein interaction, affecting the regulation of genes actively transcribed in liver cancer cells. HBx transactivates both JNK and MAPK signal transduction pathways in association with the mobilization of cytosolic Ca2+. The communication between HBx and general transcription factor TFIIB is also one of the mechanisms which account for its transcriptional transactivation. HBx decreased the expression of PTEN a known tumor suppressor and a negative regulator of phosphatidylinositol 3'-kinase/AKT and HBx decreased the expression of PTEN in HBx-transfected cells. The etiology of hepatocellular carcinoma (HCC) is involved with hepatitis B virus (HBV) infection and HBx in particular plays a role in the development of HBV-related HCC. The persistence of HBx is important to the pathogenesis of early HCC and HBx expression in the liver during chronic HBV infection may be an important prognostic marker for the development of HCC.
Stability
For long term storage lyophilized protein should be stored at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of the HBV X antigen is limited. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.
Amino Acid Sequence
MAARVCCQLD PARDVLCLRP VGAESRGRPV SGPFGTLPSP SSSAVPADHG AHLSLRGLPV CAFSSAGPCA LRFTSARRME TTVNAHQVLP KVLHKRTLGL SAMSTTDLEA YFKDCLFKDW EELGEEIRLK VFVLGGCRHK LVCSPAPCNF FTSA.

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-13 Human Recombinant, His Tag

NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

Product # :

CYT-489

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Interleukin-13 His Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (21-132) having a molecular weight of 12.84kDa with a 4kDa amino-terminal hexahistidine tag (total weight of 16.84kDa). The IL-13 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin -13 His-Tag protein is supplied in 25mM Na-Acetate (pH 4.8) and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-13 is a pleiotropic regulatory cytokine, which shares many of the properties of Interleukin-4. IL-13 is produced primarily by activated T lymphocytes and acts via specific cell surface receptor complexes. Its biological activities include the stimulation of B-cell proliferation and differentiation and the regulation of inflammatory and immune responses.
Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
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. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein has a total Mw of 12.8kDa.

What is the source or expression system of IL13 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 HUMAN, HIS Protein?
The biological functionality of IL13 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is composed from 112 amino acids.

What applications can IL13 HUMAN, HIS Protein be used in?
IL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 HUMAN, HIS Protein?
The endotoxin level is minimal, IL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 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 IL13 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:

Procalcitonin Mouse Recombinant

Calcitonin, Calca, Calc.

Product # :

HOR-014

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Procalcitonin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Ser136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

Source

Escherichia Coli.

Formulation

Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

Purity

Greater than 94.0% as determined by SDS-PAGE.

More Info

Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
Synonyms
Calcitonin, Calca, Calc.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.
Background
What is the molecular weight/Mw of PROCALCITONIN MOUSE Protein?
PROCALCITONIN MOUSE Protein has a total Mw of 13.6kDa.

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

What is the Purity of PROCALCITONIN MOUSE Protein?
PROCALCITONIN MOUSE Protein is >94% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of PROCALCITONIN MOUSE Protein?
MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.

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

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

Who supplies recombinant PROCALCITONIN 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 PROCALCITONIN 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:

Mouse Anti SARS Nucleocapsid Clone PT3851

Product # :

ANT-763

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
formulation
purity
More Info
Citations

Description

SARS Nucleoprotein antibody clone PT3851 is specific for the nucleocapsid SARS-CoV protein and recognizes the nucleoprotein of SARS-CoV-2 by ELISA.

Formulation

1mg/ml in PBS and 0.09% NaN3.

Purity

Greater than 90% as determined by SDS-PAGE gel.

More Info

Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.
Physical Appearance
Sterile Filtered liquid formulation.
Stability
Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.
Immunogen
Recombinant protein fragment 1-49 a.a. of the SARS nucleoprotein.
Clone
PT3851
Applications
ELISA.
Isotype
Mouse IgG2b.
Type
Mouse antibody Monoclonal.
Purification Method
Protein A affinity purified.

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-4 Induced-1 Human Recombinant

IL-4I1, IL4I1, IL4-I1, IL4I-1

Product # :

CYT-1209

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

IL4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (26-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 215 amino acids and having a molecular mass of 24.7kDa.IL4R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL4I1 protein solution (0.25mg/ml) contains 25mM MES pH-5.5, 40% glycerol and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

> 300 pmol/min/ug, defined as the amount of enzyme that oxidize 3-phenylpyruvate pH-7 at 25C.

More Info

Introduction
IL4I1 is a secreted L-amino acid oxidase protein that mainly catabolizes L-phenylalanine. IL4I1 eexpression is induced by the IL4 in B cells.IL4I1 is expressed in dendritic cells & macrophagesIL4I1 takes part in the immune system since it is expressed in tumor-associated macrophages and suppresses T-cell responses. IL4I1 plays a role in the binding of flavin adenine dinucleotide cofactor.
Synonyms
IL-4I1, IL4I1, IL4-I1, IL4I-1
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
ADL QDWKAER SQDPFEKCMQ DPDYEQLLKV VTWGLNRTLK PQRVIVVGAG VAGLVAAKVL SDAGHKVTIL EADNRIGGRI FTYRDQNTGW IGELGAMRMP SSHRILHKLC QGLGLNLTKF TQYDKNTWTE VHEVKLRNYV VEKVPEKLGY ALRPQEKGHS PEDIYQMALN QALKDLKALG CRKAMKKFER HTLLEYLLGE GNLSRPAVQL LGDVMSEDGF FYLSFAEALR AHSCLSDRLQ YSRIVGGWDL LPRALLSSLS GLVLLNAPVV AMTQGPHDVH VQIETSPPAR NLKVLKADVV LLTASGPAVK RITFSPPLPR HMQEALRRLH YVPATKVFLS FRRPFWREEH IEGGHSNTDR PSRMIFYPPP REGALLLASY TWSDAAAAFA GLSREEALRL ALDDVAALHG PVVRQLWDGT GVVKRWAEDQ HSQGGFVVQP PALWQTEKDD WTVPYGRIYF AGEHTAYPHG WVETAVKSAL RAAIKINSRK GPASDTASPE GHASDMEGQG HVHGVASSPS HDLAKEEGSH PPVQGQLSLQNTTHTRTSH H HHHHHH
Background
What is the molecular weight/Mw of IL 4 I1 HUMAN Protein?
IL 4 I1 HUMAN Protein has a total Mw of 24.7kDa.

What is the source or expression system of IL 4 I1 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 4 I1 HUMAN Protein?
IL 4 I1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 I1 HUMAN Protein?
> 300 pmol/min/ug, defined as the amount of enzyme that oxidize 3-phenylpyruvate pH-7 at 25C.

What is the amino acid sequence of IL 4 I1 HUMAN Protein?
ADL QDWKAER SQDPFEKCMQ DPDYEQLLKV VTWGLNRTLK PQRVIVVGAG VAGLVAAKVL SDAGHKVTIL EADNRIGGRI FTYRDQNTGW IGELGAMRMP SSHRILHKLC QGLGLNLTKF TQYDKNTWTE VHEVKLRNYV VEKVPEKLGY ALRPQEKGHS PEDIYQMALN QALKDLKALG CRKAMKKFER HTLLEYLLGE GNLSRPAVQL LGDVMSEDGF FYLSFAEALR AHSCLSDRLQ YSRIVGGWDL LPRALLSSLS GLVLLNAPVV AMTQGPHDVH VQIETSPPAR NLKVLKADVV LLTASGPAVK RITFSPPLPR HMQEALRRLH YVPATKVFLS FRRPFWREEH IEGGHSNTDR PSRMIFYPPP REGALLLASY TWSDAAAAFA GLSREEALRL ALDDVAALHG PVVRQLWDGT GVVKRWAEDQ HSQGGFVVQP PALWQTEKDD WTVPYGRIYF AGEHTAYPHG WVETAVKSAL RAAIKINSRK GPASDTASPE GHASDMEGQG HVHGVASSPS HDLAKEEGSH PPVQGQLSLQNTTHTRTSH H HHHHHH.

What applications can IL 4 I1 HUMAN Protein be used in?
IL 4 I1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 I1 HUMAN Protein?
The endotoxin level is minimal, IL 4 I1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 I1 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 IL 4 I1 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:

Interleukin-5 Receptor Alpha Human Recombinant

Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.

Product # :

cyt-1067

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IL5RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-342a.a.) and having a molecular mass of 37.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL5RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL5RA protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.
Synonyms
Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.
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
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
Background
What is the molecular weight/Mw of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein has a total Mw of 37.8kDa.

What is the source or expression system of IL 5 RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 RA HUMAN Protein?
The biological functionality of IL 5 RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 5 RA HUMAN Protein?
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
What applications can IL 5 RA HUMAN Protein be used in?
IL 5 RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 RA HUMAN Protein?
The endotoxin level is minimal, IL 5 RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 RA 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 IL 5 RA 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:

Monocyte Chemotactic Protein-1/MCAF (CCL2) Human Recombinant, HEK

CCL2, C-C motif chemokine 2, GDCF-2, HSMCR30, JE, HC11, MCAF, MCP-1, MCP1, Scya2, Sigje, SMC-CF, Immediate-early serum-responsive protein JE, Monocyte chemoattractant protein 1, Small-inducible cytokine A2.

Product # :

CHM-048

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

MCP1 Human HEK Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 82 amino acids (24-99a.a) and having a molecular mass of 9.5 kDa.MCP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The MCP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured its ability to chemoattract using THP-1 human acute monocytic leukemia cells. The ED50 range ≤ 30 ng/ml.

More Info

Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B).CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection.This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans.The cell surface receptors that bind CCL2 are CCR2 and CCR5
Synonyms
CCL2, C-C motif chemokine 2, GDCF-2, HSMCR30, JE, HC11, MCAF, MCP-1, MCP1, Scya2, Sigje, SMC-CF, Immediate-early serum-responsive protein JE, Monocyte chemoattractant protein 1, Small-inducible cytokine A2.
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
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKTHHHH HH
Background
What is the molecular weight/Mw of CCL2 HUMAN, HEK Protein?
CCL2 HUMAN, HEK Protein has a total Mw of 9.5kDa.

What is the source or expression system of CCL2 HUMAN, HEK Protein?
HEK293 Cells.

What is the Purity of CCL2 HUMAN, HEK Protein?
CCL2 HUMAN, HEK Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HEK Protein?
Measured its ability to chemoattract using THP-1 human acute monocytic leukemia cells. The ED50 range ≤ 30 ng/ml.

What is the amino acid sequence of CCL2 HUMAN, HEK Protein?
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKTHHHH HH

What applications can CCL2 HUMAN, HEK Protein be used in?
CCL2 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 HUMAN, HEK Protein?
The endotoxin level is minimal, CCL2 HUMAN, HEK Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 HUMAN, HEK 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 CCL2 HUMAN, HEK?
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:

Complement Factor I Human

Complement factor I, C3B/C4B inactivator, CFI, IF.

Product # :

PRO-2701

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Human Complement Factor I produced in Human plasma is glycosylated polypeptide composed of 2 disulfide-linked chains having a total molecular mass of 88kDa.

Source

Human Plasma.

Formulation

CFI protein solution contains Sodium phosphate, pH 7.2.

Purity

Greater than 93.0% as determined by SDS-PAGE.

More Info

Introduction
CFI cleaves and inactivates C3b and C4b. CFI is inactive without a cofactor such as the soluble factor H and C4b binding protein. CFI cleaves the alpha-peptide chain of C3b and C4b when these binds1 of the cofactors. This cleavage inactivates all of the complement activating functions of these proteins producing iC3b and iC4b.CFI cleaves the alpha chain of C3b twice and this releases a small fragment called C3f. CFI can cleave iC3b releasing C3c from C3dg in the presence of CR1.C4b is cleaved rapidly at 2 sites separating C4c from C4d.
Synonyms
Complement factor I, C3B/C4B inactivator, CFI, IF.
Physical Appearance
Sterile filtered solution.
Stability
CFI Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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 Migration Inhibitory Factor Human Recombinant

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-575

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Macrophage Inducing Factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-115aa) and having a molecular mass of 12kDa. MIF human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing 50mM Tris-HCl pH-8, 0.5mM DTT & 10% glycerol.

Purity

Greater than 98.0% as determined by SDS-PAGE.

More Info

Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

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:

Four And A Half LIM Domains 2 Human Recombinant

AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.

Product # :

PRO-2110

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

FHL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.6kDa. FHL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FHL2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Four And A Half LIM Domains 2 (FHL2) belongs to the four-and-a-half-LIM-only protein family. Family members are comprised of 2 highly conserved, tandemly arranged, zinc finger domains with 4 highly conserved cysteines binding a zinc atom in each zinc finger. The FHL2 protein is assumed to play a part in the assembly of extracellular membranes. Furthermore, FHL2 is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the FHL2 functions as a link between presenilin-2 and an intracellular signaling pathway.
Synonyms
AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
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 MGSMTERFDC HHCNESLFGK KYILREESPY CVVCFETLFA NTCEECGKPI GCDCKDLSYK DRHWHEACFH CSQCRNSLVD KPFAAKEDQL LCTDCYSNEY SSKCQECKKT IMPGTRKMEY KGSSWHETCF ICHRCQQPIG TKSFIPKDNQ NFCVPCYEKQ HAMQCVQCKK PITTGGVTYR EQPWHKECFV CTACRKQLSG QRFTARDDFA YCLNCFCDLY AKKCAGCTNP ISGLGGTKYI SFEERQWHND CFNCKKCSLS LVGRGFLTER DDILCPDCGK DI.

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:

Hepatitis C Virus NS3 Recombinant, His Tag

Product # :

HCV-267

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
formulation
purity
More Info
Citations

Description

The E.coli derived recombinant protein contains a total of 268 amino acids having a Mw of 27.9 kDa. The protein contains the HCV NS3 immunodominant regions, amino acids 1225-1456. The HCV NS3 protein is fused to a 36 His Tag at N-terminus and purified by standard chromatography techniques.

Formulation

HCV NS3 in 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.

Purity

Protein is >95% pure as determined by SDS-PAGE.

More Info

Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNA virus in the family Flaviviridae. HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host''s immune response. Hepatitis C virus is classified into six genotypes (1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Stability
HCV-NS3 His although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSVAHL HAPTGSGKST KVPAAYAAQG YKVLVLNPSV AATLGFGAYM SKAHGVDPNI RTGVRTITTG SPITYSTYGK FLADGGCSGG AYDIIICDEC HSTDATSILG IGTVLDQAET AGARLVVLAT ATPPGSVTVS HPNIEEVALS TTGEIPFYGK AIPLEVIKGG RHLIFCHSKK KCDELAAKLV ALGINAVAYY RGLDVSVIPT SGDVVVVSTD ALMTGFTGDF DSVIDCNT.

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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

SDS-PAGE

Citations

More Info

More Info

Description

Source

Formulation

Purity

SDS-PAGE

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

SDS-PAGE

Citations

More Info

More Info

Description