Search: 769 results found for "chagas"

Description:

Ig gamma-2A chain C region Mouse Recombinant

Immunoglobulin heavy chain constant region gamma 2a, Immunoglobulin G, Ig gamma-2A chain C region, A allele, Ighg.

Product # :

PRO-2842

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Description

IGHG2A Mouse Recombinant produced inSf9 Baculovirus cells is a single glycosylated polypeptide chain containing 242 amino acids (98-330 a.a.) and having a molecular mass of 27.5 kDa. IGHG2A Mouse is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IGHG2A 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.

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Synonyms
Immunoglobulin heavy chain constant region gamma 2a, Immunoglobulin G, Ig gamma-2A chain C region, A allele, Ighg.
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
ADPEPRGPTI KPCPPCKCPA PNLLGGPSVF IFPPKIKDVL MISLSPIVTC VVVDVSEDDP DVQISWFVNN VEVHTAQTQT HREDYNSTLR VVSALPIQHQ DWMSGKEFKC KVNNKDLPAP IERTISKPKG SVRAPQVYVL PPPEEEMTKK QVTLTCMVTD FMPEDIYVEW TNNGKTELNY KNTEPVLDSD GSYFMYSKLR VEKKNWVERN SYSCSVVHEG LHNHHTTKSF SRTPGKHHHH HH.
Background
The Ig gamma-2A chain C region is the constant region of the gamma-2A heavy chain in immunoglobulin molecules, particularly in mice. This region is responsible for various effector functions of IgG2a antibodies, such as antibody-dependent cellular cytotoxicity and phagocytosis and is encoded by the Ighg2a gene. The constant region of the gamma-2A chain takes part in various immune response such as regulation of the immune response, antibody-dependent cellular cytotoxicity and phagocytosis.

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:

Indian Hedgehog Human Recombinant

Indian hedgehog protein, IHH, HHG-2, BDA1.

Product # :

CYT-195

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Description

IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

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

Biological Activity

Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED₅₀ for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
Background
What is the molecular weight/Mw of IHH HUMAN Protein?
IHH HUMAN Protein has a total Mw of 19.8kDa.

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

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

What is the Biological Activity of IHH HUMAN Protein?
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

What is the amino acid sequence of IHH HUMAN Protein?
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

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

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

Exodus-2 Human Recombinant (CCL21)

Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

Product # :

CHM-332

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Shipped at Room temp

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Description

Exodus-2 Human Recombinant produced in E.Coli as a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12219 Dalton. The CCL21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM Phosphate Buffer, pH 7.4 and 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 total lymphocyte population using a concentration range of 10-100ng/ml.

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Introduction
Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.
Synonyms
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 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 Exodus2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.
Background
What is the molecular weight/Mw of CCL21 HUMAN Protein?
CCL21 HUMAN Protein has a total Mw of 12.21kDa.

What is the source or expression system of CCL21 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL21 HUMAN Protein?
CCL21 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL21 HUMAN Protein?
Determined by its ability to chemoattract human total lymphocyte population using a concentration range of 10-100ng/ml.

What is the amino acid sequence of CCL21 HUMAN Protein?
SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.

What applications can CCL21 HUMAN Protein be used in?
CCL21 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL21 HUMAN Protein?
The endotoxin level is minimal, CCL21 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL21 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 CCL21 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:

BRAK (CXCL14) Mouse Recombinant

C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

Product # :

CHM-007

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

CXCL14 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 500mM NaCl.

Purity

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

Biological Activity

The ED₅₀ of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
Background
What is the molecular weight/Mw of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein has a total Mw of 9.4kDa.

What is the source or expression system of CXCL14 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL14 MOUSE Protein?
The ED50 of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

What is the amino acid sequence of CXCL14 MOUSE Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

What applications can CXCL14 MOUSE Protein be used in?
CXCL14 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL14 MOUSE Protein?
The endotoxin level is minimal, CXCL14 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL14 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 CXCL14 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:

Thymus and Activation Regulated Chemokine (CCL17) Rat Recombinant

Thymus and activation-regulated chemokine, CCL17, SCYA17, TARC.

Product # :

CHM-012

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Quantity :

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Shipped at Room temp

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Description

TARC Rat Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 8.1kDa. The TARC Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.

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 1.0-10.0 ng/ml.

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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
Synonyms
Thymus and activation-regulated chemokine, CCL17, SCYA17, TARC.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TARC should be stored at 4C between 2-7 days and for future use below -18C. 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 TARC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ARATNVGREC CLDYFKGAIP IRKLVTWFRT SVECPKDAIV FETVQGRLIC TDPKDKHVKK AIRHLKNQRL.
Background
What is the molecular weight/Mw of CCL17 RAT Protein?
CCL17 RAT Protein has a total Mw of 8.1kDa.

What is the source or expression system of CCL17 RAT Protein?
Escherichia Coli.

What is the Purity of CCL17 RAT Protein?
CCL17 RAT Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL17 RAT Protein?
Determined by its ability to chemoattract human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml.

What is the amino acid sequence of CCL17 RAT Protein?
ARATNVGREC CLDYFKGAIP IRKLVTWFRT SVECPKDAIV FETVQGRLIC TDPKDKHVKK AIRHLKNQRL.

What applications can CCL17 RAT Protein be used in?
CCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL17 RAT Protein?
The endotoxin level is minimal, CCL17 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL17 RAT 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 CCL17 RAT?
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 Mouse Recombinant (CCL25)

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

Product # :

CHM-259

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Quantity :

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Shipped at Room temp

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Description

TECK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 14.1kDa. The TECK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.

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 CCR9 transfected BaF3 mouse pro-B cells using a concentration range of 0.1-0.5 ug/ml.

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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
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGAFEDCCLG YQHRIKWNVL RHARNYHQQE VSGSCNLRAV RFYFRQKVVC GNPEDMNVKR AIRILTARKR LVHWKSASDS QTERKKSNHM KSKVENPNST SVRSATLGHP RMVMMPRKTN N
Background
What is the molecular weight/Mw of CCL25 MOUSE Protein?
CCL25 MOUSE Protein has a total Mw of 14.1kDa.

What is the source or expression system of CCL25 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL25 MOUSE Protein?
CCL25 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL25 MOUSE Protein?
Determined by its ability to chemoattract human CCR9 transfected BaF3 mouse pro-B cells using a concentration range of 0.1-0.5 ug/ml.

What is the amino acid sequence of CCL25 MOUSE Protein?
QGAFEDCCLG YQHRIKWNVL RHARNYHQQE VSGSCNLRAV RFYFRQKVVC GNPEDMNVKR AIRILTARKR LVHWKSASDS QTERKKSNHM KSKVENPNST SVRSATLGHP RMVMMPRKTN N

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

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

Who supplies recombinant CCL25 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 CCL25 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:

Phosphoglycerate Mutase 1 Mouse Recombinant

Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

Product # :

ENZ-627

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
Physical Appearance
Sterile Filtered clear 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 MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.

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:

Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant

Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.

Product # :

PRO-1721

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Shipped with Ice Packs

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Description

CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.

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 Mouse 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-336

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Quantity :

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Description

IP-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8701 Dalton. The IP-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IP-10 was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

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 hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

sds-page

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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. 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
IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.
Background
What is the molecular weight/Mw of CXCL10 MOUSE Protein?
CXCL10 MOUSE Protein has a total Mw of 8.7kDa.

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

What is the Purity of CXCL10 MOUSE Protein?
CXCL10 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 MOUSE Protein?
Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

What is the amino acid sequence of CXCL10 MOUSE Protein?
IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

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

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

Who supplies recombinant CXCL10 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.02 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 IP-10 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:

Monocyte Chemotactic Protein-2 Mouse Recombinant (CCL8)

Small inducible cytokine A8, CCL8, Monocyte chemotactic protein 2, MCP-2, Monocyte chemoattractant protein 2, HC14, chemokine (C-C motif) ligand 8, MCP2, SCYA8, SCYA10, AB023418, 1810063B20Rik.

Product # :

CHM-355

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Quantity :

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Description

Monocyte Chemotactic Protein-2 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 74 amino acids and having a molecular mass of 8507 Dalton. The MCP-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, 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 monocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Chemokine (C-C motif) ligand 8 (CCL8) is a small cytokine belonging to the CC chemokine family that was once called monocyte chemotactic protein-2 (MCP-2). The CCL8 protein is produced as a precursor containing 109 amino acids, which is cleaved to produce mature CCL8 containing 75 amino acids. The gene for CCL8 is encoded by 3 exons and is located within a large cluster of CC chemokines on chromosome 17q11.2 in humans. MCP-2 is chemotactic for and activates a many different immune cells, including mast cells, eosinophils and basophils, (that are implicated in allergic responses), and monocytes, T cells, and NK cells that are involved in the inflammatory response. CCL8 elicits its effects by binding to several different cell surface receptors called chemokine receptors. These receptors include CCR1, CCR2B and CCR5.
Synonyms
Small inducible cytokine A8, CCL8, Monocyte chemotactic protein 2, MCP-2, Monocyte chemoattractant protein 2, HC14, chemokine (C-C motif) ligand 8, MCP2, SCYA8, SCYA10, AB023418, 1810063B20Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL8 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 CCL8in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPDKAPVTCC FHVLKLKIPL RVLKSYERIN NIQCPMEAVV FQTKQGMSLC VDPTQKWVSE YMEILDQKSQ ILQP.
Background
What is the molecular weight/Mw of CCL8 MOUSE Protein?
CCL8 MOUSE Protein has a total Mw of 8.5kDa.

What is the source or expression system of CCL8 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL8 MOUSE Protein?
CCL8 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL8 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood monocytes 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 CCL8 MOUSE Protein?
GPDKAPVTCC FHVLKLKIPL RVLKSYERIN NIQCPMEAVV FQTKQGMSLC VDPTQKWVSE YMEILDQKSQ ILQP.

What applications can CCL8 MOUSE Protein be used in?
CCL8 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL8 MOUSE Protein?
The endotoxin level is minimal, CCL8 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL8 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 CCL8 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 Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

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

Product # :

CYT-431

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Description

MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing 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
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 colorless solution.
Stability
Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

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:

Stromal Cell-Derived Factor-1 beta Feline Recombinant (CXCL12)

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

Product # :

CHM-247

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Quantity :

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Description

Stromal Cell-Derived Factor-1 beta Feline Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8526 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.

Purity

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

Biological Activity

The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

More Info

Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.
Background
What is the molecular weight/Mw of CXCL12 FELINE BETA Protein?
CXCL12 FELINE BETA Protein has a total Mw of 8.5kDa.

What is the source or expression system of CXCL12 FELINE BETA Protein?
Escherichia Coli.

What is the Purity of CXCL12 FELINE BETA Protein?
CXCL12 FELINE BETA Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 FELINE BETA Protein?
The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

What is the amino acid sequence of CXCL12 FELINE BETA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.

What applications can CXCL12 FELINE BETA Protein be used in?
CXCL12 FELINE BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 FELINE BETA Protein?
The endotoxin level is minimal, CXCL12 FELINE BETA Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 FELINE BETA 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 CXCL12 FELINE BETA?
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-Gamma Equine Recombinant

Interferon gamma, IFN-gamma, IFNG.

Product # :

CYT-739

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Description

Recombinant Equine Interferon-gamma produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 143 amino acids and having a molecular mass of 16.7kDa.The IFN-gamma Equine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 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.

Biological Activity

The ED₅₀ as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁵ IU/mg.

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
Interferon gamma, IFN-gamma, IFNG.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interferon-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 Interferon-gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ.
Background
What is the molecular weight/Mw of IFNG EQUINE Protein?
IFNG EQUINE Protein has a total Mw of 16.7kDa.

What is the source or expression system of IFNG EQUINE Protein?
Escherichia Coli.

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

What is the Biological Activity of IFNG EQUINE Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

What is the amino acid sequence of IFNG EQUINE Protein?
QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ.
What applications can IFNG EQUINE Protein be used in?
IFNG EQUINE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Interferon-Gamma Human Recombinant, His Tag

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

Product # :

CYT-478

Price :

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Description

IFN-Gamma Human Recombinant produced in E.Coli is a single, glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) without cysteine residues and having a molecular mass of 18.5kDa (confirmed by MALDI-TOF). IFN-Gamma is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interferon-g is supplied in phosphate-buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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 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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
Background
What is the molecular weight/Mw of IFNG HUMAN, HIS Protein?
IFNG HUMAN, HIS Protein has a total Mw of 18.5kDa.

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

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

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

What is the amino acid sequence of IFNG HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

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

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

H1N1 Influenza A- Virus Puerto Rico 08/1934 Recombinant

Product # :

IHA-036

Price :

Quantity :

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Description

Recombinant Full-Length H1N1 Puerto Rico 08/1934 is glycosylated with N-linked sugars, produced using baculovirus vectors in insect cells and its Mw is approximately 62 kDa.

Source

Baculovirus Insect Cells.

Formulation

The Recombinant H1N1 A/Puerto Rico 08/1934 solution contains 10mM Sodium phosphate, pH 7.2, 150mM NaCl and 0.005% Tween-20.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
H1N1 is a subtype specie of Influenza A virus. H1N1 Influenza Virus has mutated into various strains such as the Spanish Flustrain, mild humanflu strains, endemic pigstrains, and various strains found in birds. The Influenza A Virus is a globular particle about 100nm in diameter, sheathed in a lipid bilayer derived from the plasma membrane of its host. Studded in the lipid bilayer are two integral membrane proteins some 500 molecules of hemagglutinin ("H") and some 100 molecules of neuraminidase ("N"). Within the lipid bilayer are 3000 molecules of matrix protein and 8 pieces of RNA. Each of the 8 RNA molecules is associated with many copies of a nucleoprotein, several molecules of the three subunits of its RNA polymerase some "non-structural" protein molecules of uncertain function.
Physical Appearance
Sterile Filtered colorless solution.
Stability
H1N1 A/Puerto Rico 08/1934 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:

Galectin-3 Mouse Recombinant, BioActive

Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.

Product # :

CYT-1151

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Description

LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

LGALS3 protein (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol,1mM DTT and 2mM EDTA.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

sds-page

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Introduction
Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.
Synonyms
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
Background
What is the molecular weight/Mw of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein has a total Mw of 29.8kDa.

What is the source or expression system of LGALS3 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS3 MOUSE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

What is the amino acid sequence of LGALS3 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.

What applications can LGALS3 MOUSE Protein be used in?
LGALS3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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:

Dengue Virus Subtype-2 Envelope 22kDa Recombinant

Product # :

DEN-007

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Description

The E.coli derived recombinant 22 kDa protein is genetically engineered peptide which is derived from Dengue Type-2 Envelope. This region also contains a common antigen for Dengue IgG & IgM. This protein is fused to 6xHis tag.

Source

Escherichia Coli.

Formulation

Phosphorous buffered saline, pH-7.4.

Purity

Protein is >95% pure as determined by 12% PAGE (coomassie staining).

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Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
Stability
Dengue Envelope ST2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Each laboratory should determine an optimum working titer for use in its particular application.
Purification Method
Purified by proprietary chromatographic technique.

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:

Tick-Borne Encephalitis Virus gE Middle Recombinant

Product # :

TBE-283

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Description

The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus glycoprotein E middle regions, 50-250 amino acids.

Source

Escherichia Coli.

Formulation

20mM MES pH 6.5, 8M urea, 200mM NaCl and 0.05% Tween-20.

Purity

Encephalitis protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
TBE is caused by tick-borne encephalitis virus (TBEV), a member of the family Flaviviridae.
A closely related virus in Far Eastern Eurasia, Russian spring-summer encephalitis virus (RSSEV).
The family Flaviviridae includes other tick-borne viruses are closely related to TBEV and RSSEV, such as Omsk hemorrhagic fever virus & Kyasanur Forest virus.
Louping ill virus is also a member of this family.
Physical Appearance
Sterile Filtered clear solution.
Stability
Encephalitis protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Encephalitis antigen is suitable for ELISA and Western blots, excellent antigen for detection of Tick-borne encephalitis virus with minimal specificity problems.
Specificity
Immunoreactive with sera of encephalitis virus infected individuals.
Purification Method
Encephalitis protein was purified by proprietary chromatographic technique.

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:

Acetylcholinesterase Human Recombinant

AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6

Product # :

ENZ-1174

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Description

ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa. ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The ACHE solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 6,000 nmol/min/ug. Defined by the amount of enzyme that cleaves 1 nmole of acetylthiocholine per minute at pH 7.5 at 25˚C.

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Introduction
Acetylcholinesterase (ACHE) belongs to the type-B carboxylesterase/lipase family. ACHE catalyzes the breakdown of acetylcholine and other choline esters that play a role as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds ACH receptors on the post-synaptic membrane, transmitting the signal from the nerve. ACHE is located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH.
Synonyms
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
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
DGSEGREDAE LLVTVRGGRL RGIRLKTPGG PVSAFLGIPF AEPPMGPRRF LPPEPKQPWS GVVDATTFQS VCYQYVDTLY PGFEGTEMWN PNRELSEDCL YLNVWTPYPR PTSPTPVLVW IYGGGFYSGA SSLDVYDGRF LVQAERTVLV SMNYRVGAFG FLALPGSREA PGNVGLLDQR LALQWVQENV AAFGGDPTSV TLFGESAGAA SVGMHLLSPP SRGLFHRAVL QSGAPNGPWA TVGMGEARRR ATQLAHLVGC PPGGTGGNDT ELVACLRTRP AQVLVNHEWH VLPQESVFRF SFVPVVDGDF LSDTPEALIN AGDFHGLQVL VGVVKDEGSY FLVYGAPGFS KDNESLISRA EFLAGVRVGV PQVSDLAAEA VVLHYTDWLH PEDPARLREA LSDVVGDHNV VCPVAQLAGR LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDLHHHH 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.

Description:

Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

Product # :

CHM-323

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Description

SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.
Background
What is the molecular weight/Mw of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein has a total Mw of 10.4kDa.

What is the source or expression system of CXCL12 MOUSE ALPHA, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 MOUSE ALPHA, HIS Protein?
The biological functionality of CXCL12 MOUSE ALPHA, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL12 MOUSE ALPHA, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

What applications can CXCL12 MOUSE ALPHA, HIS Protein be used in?
CXCL12 MOUSE ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 MOUSE ALPHA, HIS Protein?
The endotoxin level is minimal, CXCL12 MOUSE ALPHA, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 MOUSE ALPHA, 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 CXCL12 MOUSE ALPHA, 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:

Asparaginyl-TRNA Synthetase Human Recombinant

NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

Product # :

ENZ-915

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Description

NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.
Synonyms
NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.
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
GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

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:

Arylsulfatase A Human Recombinant, Sf9

Arylsulfatase A, Cerebroside-Sulfatase, ASA, Metachromatic Leucodystrophy, MLD, EC 3.1.6.8.

Product # :

ENZ-1087

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Description

ARSA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 498 amino acids (21-509a.a.) and having a molecular mass of 53.0kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ARSA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ARSA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 2,500 pmol/min/ug, and defined as the amount of enzyme that hydrolyze 4-Nitrocatechol at pH 5.0 at 37C.

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Introduction
The enzyme Arylsulfatase A, also known as cerebroside-sulfatase, is responsible to break down sulfatides. The main molecule that Arylsulfatase A breaks down is cerebroside 3-sulfate into cerebroside and sulfate. The enzyme is encoded by the ARSA gene in humans. Phosphate can form a covalent bond with the Arylsulfatase A’s active site 3-oxoalanine, thus, inhibits the protein.
Synonyms
Arylsulfatase A, Cerebroside-Sulfatase, ASA, Metachromatic Leucodystrophy, MLD, EC 3.1.6.8.
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
ADPRPPNIVL IFADDLGYGD LGCYGHPSST TPNLDQLAAG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRM GMYPGVLVPS SRGGLPLEEVTVAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPA TPCDGGCDQG LVPIPLLANL SVEAQPPWLP GLEARYMAFA HDLMADAQRQ DRPFFLYYAS HHTHYPQFSG QSFAERSGRG PFGDSLMELD AAVGTLMTAI GDLGLLEETL VIFTADNGPETMRMSRGGCS GLLRCGKGTT YEGGVREPAL AFWPGHIAPG VTHELASSLD LLPTLAALAG APLPNVTLDG FDLSPLLLGT GKSPRQSLFF YPSYPDEVRG VFAVRTGKYK AHFFTQGSAH SDTTADPACH ASSSLTAHEP PLLYDLSKDP GENYNLLGGV AGATPEVLQA LKQLQLLKAQLDAAVTFGPS QVARGEDPAL QICCHPGCTP RPACCHCPDP HAHHHHHH.

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:

Arylsulfatase A Mouse Recombinant, Active

Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.

Product # :

ENZ-1088

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Description

ARSA Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 498 amino acids (18-506) and having a molecular mass of 53.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ARSA Mouse is fused to an 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ARSA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.
Synonyms
Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.
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
ADPSPPNILL IFADDLGYGD LGSYGHPSST TPNLDQLAEG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRSGMYPGVLGPS SQGGLPLEEVTLAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPD IPCKGGCDQG LVPIPLLANL TVEAQPPWLPGLEARYVSFS RDLMADAQRQ GRPFFLYYAS HHTHYPQFSG QSFTKRSGRG PFGDSLMELD GAVGALMTTV GDLGLLEETL VIFTADNGPELMRMSNGGCSGLLRCGKGTT FEGGVREPAL VYWPGHITPG VTHELASSLD LLPTLAALTG APLPNVTLDG VDISPLLLGT GKSPRKSVFFYPPYPDEIHG VFAVRNGKYK AHFFTQGSAH SDTTSDPACH AANRLTAHEP PLLYDLSQDP GENYNVLESI EGVSPEALQA LKHIQLLKAQYDAAMTFGPS QIAKGEDPAL QICCQPSCTP HPVCCHCPGS QSHHHHHH.

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:

CD3G Human Recombinant, Sf9

T-cell surface glycoprotein CD3 gamma chain, CD3-GAMMA, T3G, CD3G

Product # :

PRO-2412

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Description

CD3G Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (23-116 a.a.) and having a molecular mass of 11.8kDa.CD3G is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CD3G protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
CD3-gamma polypeptide is encoded by CD3 Gamma (CD3G) which together with CD3-epsilon, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, configures the T-cell receptor-CD3 complex. The T-cell receptor-CD3 complex takes part in coupling antigen recognition to numerous intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. Deficiencies in this gene are associated with T cell immunodeficiency.
Synonyms
T-cell surface glycoprotein CD3 gamma chain, CD3-GAMMA, T3G, CD3G
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
ADPQSIKGNH LVKVYDYQED GSVLLTCDAE AKNITWFKDG KMIGFLTEDK KKWNLGSNAK DPRGMYQCKG SQNKSKPLQV YYRMCQNCIE LNAATISHHH HHH.

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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