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Description:

Interleukin-8 Canine Recombinant

Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.

Product # :

CHM-009

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Shipped at Room temp

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Description

Interleukin-8 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa. The IL8 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

The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.
Background
What is the molecular weight/Mw of CXCL8 CANINE Protein?
CXCL8 CANINE Protein has a total Mw of 9.1kDa.

What is the source or expression system of CXCL8 CANINE Protein?
Escherichia Coli.

What is the Purity of CXCL8 CANINE Protein?
CXCL8 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 CANINE Protein?
The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

What is the amino acid sequence of CXCL8 CANINE Protein?
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.

What applications can CXCL8 CANINE Protein be used in?
CXCL8 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 CANINE Protein?
The endotoxin level is minimal, CXCL8 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 CANINE 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 CXCL8 CANINE?
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-8 Rhesus Macaque Recombinant

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP

Product # :

CHM-004

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Shipped at Room temp

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Description

IL 8 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa.The IL 8 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

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-8 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-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP
Background
What is the molecular weight/Mw of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein has a total Mw of 9.1kDa.

What is the source or expression system of CXCL8 MACAQUE Protein?
Escherichia Coli.

What is the Purity of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 MACAQUE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

What is the amino acid sequence of CXCL8 MACAQUE Protein?
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

What applications can CXCL8 MACAQUE Protein be used in?
CXCL8 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 MACAQUE Protein?
The endotoxin level is minimal, CXCL8 MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 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 CXCL8 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:

Fractalkine Human Recombinant (CX3CL1)

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-235

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Shipped at Room temp

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Description

Fractalkine Human Recombinant- produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8638 Dalton. The Fractalkine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CX3CL1 was lyophilized from a 0.2μm filtered concentrated (1.0 mg/ml) solution in 20mM Phosphate buffer, pH 7.4, 50mM NaCl.

Purity

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

Biological Activity

The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.
Background
What is the molecular weight/Mw of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein has a total Mw of 8.63kDa.

What is the source or expression system of CX3CL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

What is the amino acid sequence of CX3CL1 HUMAN Protein?
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

What applications can CX3CL1 HUMAN Protein be used in?
CX3CL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN Protein?
The endotoxin level is minimal, CX3CL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CX3CL1 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 CX3CL1 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:

LAG-1 (CCL4L1) Human Recombinant, His Tag

C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.

Product # :

CHM-272

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Shipped with Ice Packs

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Description

LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (24-92 a.a.) and having a molecular mass of 10.5kDa (Molecular weight on SDS-PAGE will appear higher).LAG-1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LAG-1 protein solution (0.5mg/ml) containing 10mM sodium citrate (pH 3.5) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
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 MGSHMAPMGS DPPTACCFSY TARKLPRNFV VDYYETSSLC SQPAVVFQTK RGKQVCADPS ESWVQEYVYD LELN.
Background
What is the molecular weight/Mw of CCL4L1 HUMAN, HIS Protein?
CCL4L1 HUMAN, HIS Protein has a total Mw of 10.5kDa.

What is the source or expression system of CCL4L1 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL4L1 HUMAN, HIS Protein?
CCL4L1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL4L1 HUMAN, HIS Protein?
The biological functionality of CCL4L1 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL4L1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPMGS DPPTACCFSY TARKLPRNFV VDYYETSSLC SQPAVVFQTK RGKQVCADPS ESWVQEYVYD LELN.

What applications can CCL4L1 HUMAN, HIS Protein be used in?
CCL4L1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL4L1 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL4L1 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL4L1 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 CCL4L1 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:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2)

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

Product # :

CHM-271

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Quantity :

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Shipped at Room temp

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Description

Monocyte Chemotactic Protein-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 8.6kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCL2 was lyophilized from a concentrated (1mg/ml) sterile solution without any additives.

Purity

Greater than 98.0% as determined by RP-HPLC and SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

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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
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 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 Monocyte Chemotactic Protein-1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN Protein?
CCL2 HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of CCL2 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL2 HUMAN Protein?
CCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN Protein?
The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

What is the amino acid sequence of CCL2 HUMAN Protein?
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

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

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

Who supplies recombinant CCL2 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 CCL2 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:

Macrophage-Derived Chemokine Human Recombinant (CCL22)

C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

Product # :

CHM-250

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 8.1 kDa. The MDC is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCL22 filtered (0.4µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 500mM NaCl 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 human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.
Background
What is the molecular weight/Mw of CCL22 HUMAN Protein?
CCL22 HUMAN Protein has a total Mw of 8.1kDa.

What is the source or expression system of CCL22 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL22 HUMAN Protein?
CCL22 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL22 HUMAN Protein?
Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL22 HUMAN Protein?
GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

What applications can CCL22 HUMAN Protein be used in?
CCL22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL22 HUMAN Protein?
The endotoxin level is minimal, CCL22 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:

Macrophage-Derived Chemokine (CCL22) Rat Recombinant

C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

Product # :

CHM-279

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

CCL22 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9kDa. The Rat CCL22 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 activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

More Info

Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MDC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MDC 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 MDC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA.
Background
What is the molecular weight/Mw of CCL22 RAT Protein?
CCL22 RAT Protein has a total Mw of 7.9kDa.

What is the source or expression system of CCL22 RAT Protein?
Escherichia Coli.

What is the Purity of CCL22 RAT Protein?
CCL22 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL22 RAT Protein?
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CCL22 RAT Protein?
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA

What applications can CCL22 RAT Protein be used in?
CCL22 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL22 RAT Protein?
The endotoxin level is minimal, CCL22 RAT 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-8 (1-72 a.a.) Human Recombinant (CXCL8)

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

Product # :

CHM-231

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Quantity :

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Citations

Description

Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

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

Biological Activity

Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

sds-page

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.

What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
Escherichia Coli.

What is the Purity of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.

What applications can CXCL8 HUMAN (1-72) Protein be used in?
CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-72) Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 HUMAN (1-72) 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 CXCL8 HUMAN (1-72)?
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:

CD52 Human Recombinant

CD52 Molecule, Human Epididymis-Specific Protein 5, CD52 Antigen, Epididymal Secretory Protein E5, Cambridge Pathology 1 Antigen, CDW52, He5, Epididymis Secretory Sperm Binding Protein Li 171mP, CDW52 Antigen, CD52 Antigen, HEL-S-171mP, EDDM5, CDw52, HE5.

Product # :

PRO-2525

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Description

CD52 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 251 amino acids (25-36 a.a.) and having a molecular mass of 28.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD52 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CD52 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
CD52 is a small GPI (glycosylphosphatidylinositol) anchored glycoprotein which is tied to the cell surface with a GPI linkage. CD52 induces immune suppression by complement-meditated cell lysis. Moreover, CD52 is expressed on lymphocytes, eosinophils, monocytes-derived dendritic cells, monocytes, as well as neutrophils, however not on the stem cells from which these lymphocytes were derived. Furthermore, CD52 is a significant goal for therapeutic interventions intended for leukocyte depletion in post-transplant immunosuppression & hematological malignancies.
Synonyms
CD52 Molecule, Human Epididymis-Specific Protein 5, CD52 Antigen, Epididymal Secretory Protein E5, Cambridge Pathology 1 Antigen, CDW52, He5, Epididymis Secretory Sperm Binding Protein Li 171mP, CDW52 Antigen, CD52 Antigen, HEL-S-171mP, EDDM5, CDw52, HE5.
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
GQNDTSQTSS PSLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE
SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

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:

Uridine Phosphorylase Salmonella Typhimurium Recombinant

Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.

Product # :

ENZ-348

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Description

Uridine phosphorylase Salmonella typhimurium Recombinantproduced in E.Coli is a non-glycosylated, polypeptide having a total molecular mass of 163068 Dalton.

Source

Escherichia Coli.

Formulation

The UPase was lyophilized from 1mg/ml solution containing 25mM Tris-HCl, pH 8.0, 0.15M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.
Synonyms
Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized UPase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UPase 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 UPase in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Enzymatic Activity
30 U/mg protein.
Unit Definition
One unit phosphorylates 1μm of uridine within 1 min at pH 7.3.

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.

Uridine Phosphorylase Salmonella Typhimurium

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

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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:

HIV-1 nef Clade B Recombinant

Product # :

HIV-156

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Quantity :

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Description

The E.coli derived 27 kDa recombinant HIV-1 Nef Clade-B protein is a single non-glycosylated polypeptide chain.

Source

Escherichia Coli.

Formulation

Lyophilized with 1% glycerol.

Purity

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

More Info

Introduction
HIV-1 Nef is a 27kDa protein highly produced after a very short time after virus infection. HIV-1 Nef is an essential factor for efficient viral replication and phatogenesis.
HIV-1 Nef facilitates virus replication and improves virions infectivity. HIV-1 Nef exerts pleiotropic effect. HIV-1 Nef down-modulates surface MHC-I molecules, decreases cell surface CD4 antigen by interacting with the Src family kinase LCK thereby inducing LCK-CD4 dissociation and by increasing clathrindependent endocytosis of this antigen to target it to lysosomial degradation. HIV-1 Nef guards the infected cell from apoptosis in order to keep it alive until the next virus generation is ready to strike. HIV-1 Nef protein bypasses host Tcell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation.
Physical Appearance
Sterile Filtered and lyophilized, though might appear as a solution as a result of the glycerol content.
Stability
Lyophilized HIV-1 nef although stable at room temperature for 1 week, should be stored desiccated below -18°C. Upon reconstitution HIV-1 nef 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 HIV-1 nef in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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:

MYC Associated Factor X Human Recombinant

bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.

Product # :

PRO-811

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Description

MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
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
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.

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:

Dnak Substrate Binding Domain C-terminal E.Coli Recombinant

HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

Product # :

HSP-009

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Description

Recombinant Dnak Substrate Binding Domain C-terminal produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids and having a molecular mass of 27.7 kDa.

Source

Escherichia Coli.

Formulation

The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
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
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQGERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKTAIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK.

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

Description:

Macrophage Inflammatory Protein-1 Gamma Mouse Recombinant (CCL9)

CCL9/10, MRP2, CCF18.

Product # :

CHM-257

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Description

MIP-1 gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 101 amino acids and having a molecular mass of 11.6 kDa. The MIP-1 gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MIP-1 gamma was lyophilized from 1xPBS solution pH-7.4.

Purity

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

Biological Activity

Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.
Synonyms
CCL9/10, MRP2, CCF18.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-1 gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL9/10 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 MIP-1 gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.
Background
What is the molecular weight/Mw of CCL9 MOUSE Protein?
CCL9 MOUSE Protein has a total Mw of 11.6kDa.

What is the source or expression system of CCL9 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL9 MOUSE Protein?
CCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL9 MOUSE Protein?
Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL9 MOUSE Protein?
QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

What applications can CCL9 MOUSE Protein be used in?
CCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL9 MOUSE Protein?
The endotoxin level is minimal, CCL9 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

I-309 Human Recombinant (CCL1)

Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

Product # :

CHM-312

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Quantity :

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Shipped at Room temp

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Description

I-309 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8504 Dalton. The I-309 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL1 protein was lyophilized with no additives.

Purity

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

Biological Activity

The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.
Synonyms
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized I-309 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL1 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 I-309 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.
Background
What is the molecular weight/Mw of CCL1 HUMAN Protein?
CCL1 HUMAN Protein has a total Mw of 8.5kDa.

What is the source or expression system of CCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL1 HUMAN Protein?
CCL1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.

What applications can CCL1 HUMAN Protein be used in?
CCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL1 HUMAN Protein?
The endotoxin level is minimal, CCL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL1 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 CCL1 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:

Yersinia Enterocolitica (O:9) YopN Recombinant

Product # :

PRO-2274

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Description

Recombinant Yersinia Enterocolitica (O:9) YopN produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 34,296 Dalton. Y.Enterocolitica (O:9) YopN is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Y.Enterocolitica (O:9) YopN is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

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-1/2 ELISA Recombinant

Product # :

HIV-019

Price :

Quantity :

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Description

Paired HIV antigens for ELISA test contain HIV1 gp41 and HIV2 gp36 which are used to detect HIV1 and HIV2 antibody from the infected patients. Please note that when ordering for example: 100µg HIV-1/2 ELISA we ship 50µg from each of the antibodies (100µg in total).

Source

Escherichia Coli.

Formulation

* HIV1 gp41 in 25mM K2CO3 and PBS.

* HIV2 gp36 in 25mM K2CO3 and PBS.

Purity

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

More Info

Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Stability
For periods up to 1 month HIV-1/2 Rapid should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Background
Recombinant HIV-1/2 Proteins play a crucial role in antiviral drug development. They serve as targets for drug screening, allowing researchers to identify compounds that inhibit key viral enzymes or interfere with viral entry. Moreover, these proteins are instrumental in studying drug resistance mechanisms, providing insights into how the virus adapts to selective pressures and guiding the development of more effective antiretroviral therapies.

Understanding Viral Dynamics and Host Interactions:
Studying Recombinant HIV-1/2 Proteins provides a lens into the dynamic interplay between the virus and host cells. These proteins help unravel the mechanisms of viral entry, integration into the host genome, and evasion of host immune surveillance. Insights gained from these studies are critical for devising strategies to disrupt viral replication and enhance the host's ability to control or eliminate the virus.

Challenges and Future Directions:
While the potential of Recombinant HIV-1/2 Proteins in HIV research is evident, challenges persist. Fine-tuning their applications, addressing issues of genetic diversity within HIV subtypes, and optimizing strategies for vaccine and drug development are critical considerations for translational success. Additionally, understanding the intricate host-virus interactions in different cellular contexts remains a dynamic area of investigation.
Recombinant HIV-1/2 Proteins stand as sentinel tools in the ongoing battle against HIV/AIDS, providing researchers with a nuanced understanding of viral dynamics and immune responses. Their structural insights, immunogenic properties, and applications in drug and vaccine development position them as central players in advancing our capabilities to combat HIV. As scientists continue to delve into the molecular intricacies of these recombinant proteins, they not only deepen our understanding of HIV pathogenesis but also pave the way for transformative advancements in HIV treatment and prevention, shaping the future of global health efforts against this formidable virus.

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 Zika NS1 Paired

Product # :

ANT-008

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Description

Zika NS1 conjugation antibody and Zika NS1 capture antibody are used to develop rapid test for Zika NS1 rapid test. Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).

Formulation

* Zika NS1 gold conjugation antibody in PBS, 10mg BSA/ml & 0.1% Sodium Nitrate.
* Zika NS1 capture antibody in PBS, 10mg BSA/ml & 0.1% Sodium Nitrate.

Purity

Greater than 95%.

More Info

Introduction
Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.
Physical Appearance
2 vials of sterile filtered clear colorless solution.
Stability
Zika antibody although stable at 4°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.
Applications
Lateral flow immunoassay.
Type
Mouse antibody Monoclonal.
Purification Method
Purified monoclonal IgG by protein A chromatography.

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:

Borrelia Afzelii Outer Surface Protein p100 Recombinant

Product # :

BOR-017

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Quantity :

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Description

Recombinant Borrelia Afzelii Outer Surface Protein p100 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 74,782 Dalton. Borrelia Afzelii p100 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Borrelia Afzelii p100 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

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

Description:

Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)

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

Product # :

CHM-233

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 0.55 mg/ml solution containing no additives.

Purity

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

Biological Activity

The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

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

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

What is the Purity of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of MIP 1A HUMAN Protein?
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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

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

What is the endotoxin level for MIP 1A HUMAN Protein?
The endotoxin level is minimal, MIP 1A 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:

Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)

MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

Product # :

CHM-369

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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biological activity
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Description

CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 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 mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.

What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.

What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

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

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biological activity
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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:

Lymphotactin (XCL1) Rat 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-038

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Lymphotactin (XCL1) Rat Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.0kDa.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 < 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
VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.
Background
What is the molecular weight/Mw of LYMPHOTACTIN RAT Protein?
LYMPHOTACTIN RAT Protein has a total Mw of 10kDa.

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

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

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

What is the amino acid sequence of LYMPHOTACTIN RAT Protein?
VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.

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

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

Who supplies recombinant LYMPHOTACTIN 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 LYMPHOTACTIN 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.

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