Search: 1000 results found for "Anti Mouse Cytokine"

Description:

B-cell Activating Factor Human Recombinant

BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

Product # :

CYT-307

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Description

BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

Purity

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

Biological Activity

The activity is determined by a mouse splenocyte survival assay. The ED₅₀ for this effect is 0.5-2.0µg/ml.

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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 17.7kDa.

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

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

What is the Biological Activity of BLYS Protein?
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

What is the amino acid sequence of BLYS Protein?
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

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

What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 139 a.a Human Recombinant

Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.

Product # :

CYT-843

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Description

IFNG 139 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (24-161 a.a.) and having a molecular mass of 16.3kDa. IFNG 139 a.a. is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNG 139 a.a. protein solution (1mg/ml) contains PBS buffer (pH 7.4) and 10% glycerol.

Purity

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

Biological Activity

IFNG activity was wmasured in a cytotoxicity assay using WiDr cells. The ED50 was found to be less or equal to 0.5ng/ml.

SDS-PAGE

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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 interferons.
Synonyms
Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon 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
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
Background
What is the molecular weight/Mw of IFNG 139 A.A. HUMAN Protein?
IFNG 139 A.A. HUMAN Protein has a total Mw of 16.3kDa.

What is the source or expression system of IFNG 139 A.A. HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNG 139 A.A. HUMAN Protein?
IFNG 139 A.A. HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNG 139 A.A. HUMAN Protein?
IFNG activity was wmasured in a cytotoxicity assay using WiDr cells. The ED50 was found to be less or equal to 0.5ng/ml.

What is the amino acid sequence of IFNG 139 A.A. HUMAN Protein?
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

What applications can IFNG 139 A.A. HUMAN Protein be used in?
IFNG 139 A.A. HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNG 139 A.A. HUMAN Protein?
The endotoxin level is minimal, IFNG 139 A.A. 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:

Thymic Stromal Lymphopoietin Human Recombinant, His Tag

Thymic Stromal Lymphopoietin, TSLP.

Product # :

CYT-836

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Description

TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr29-Gln159) containing 141 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16.2kDa.

Source

Escherichia Coli.

Formulation

TSLP was filtered (0.4µm) and lyophilized in phosphate buffered saline.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.
Synonyms
Thymic Stromal Lymphopoietin, TSLP.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. TSLP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASYDFTNCDFEK IKAAYLSTIS KDLITYMSGT KSTEFNNTVS CSNRPHCLTE IQSLTFNPTA GCASLAKEMF AMKTKAALAI WCPGYSETQI NATQAMKKRR KRKVTTNKCL EQVSQLQGLW RRFNRPLLKQ Q.

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:

Allograft Inflammatory Factor 1 Like Human Recombinant

Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.

Product # :

CYT-007

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Description

AIF1L produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150a.a.) and having a molecular mass of 19.2kDa.AIF1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIF1L protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

sds-page

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Synonyms
Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.
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 MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.
Background
Allograft Inflammatory Factor 1-Like Human Recombinant: Investigating its Role in Immune Responses and Potential Therapeutic Applications
1. Abstract
This paper seeks to provide an in-depth overview of Allograft Inflammatory Factor 1-Like Human Recombinant (AIF-1L), a significant protein involved in the regulation of inflammatory responses. By delving into the structure, biological functions, and pathological implications of AIF-1L, we attempt to shed light on its potential as a therapeutic target in immune-mediated disorders.
2. Introduction
AIF-1L belongs to the allograft inflammatory factor protein family and is implicated in immune responses. With its intricate interaction with a multitude of immune cells and involvement in various inflammatory and immune-related diseases, it serves as a pivotal point of interest for therapeutic intervention research.
3. Structure and Signaling of AIF-1L
AIF-1L shares a conserved EF-hand calcium-binding motif with its counterpart AIF-1, suggesting similar calcium-dependent activities. While its signaling pathway remains largely elusive, the protein is believed to modulate macrophage activation, an integral part of immune response regulation.
4. Biological Functions of AIF-1L
AIF-1L is fundamentally involved in immune response modulation, especially in the context of macrophage activation. It plays key roles in managing inflammation, cell proliferation, survival, and differentiation.
5. AIF-1L in Disease Pathology
AIF-1L is linked with a range of inflammatory and immune-related disorders, including but not limited to rheumatoid arthritis, atherosclerosis, and certain cancers. This association underscores its profound physiological relevance and potential as a therapeutic target.
6. Therapeutic Potential of AIF-1L
Given its central role in immune responses, AIF-1L presents a promising target for therapeutic strategies. Manipulating AIF-1L activity could pave the way for novel treatments of various inflammatory and immune-mediated diseases.
7. Conclusion and Future Perspectives
Though our comprehension of AIF-1L has made significant strides, there is still much terrain left to explore. Future research directed at the precise molecular mechanisms and pathological roles of AIF-1L will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1L Protein?
AIF1L Protein has a total Mw of 19.2kDa.

What is the source or expression system of AIF1L Protein?
Escherichia Coli.

What is the Purity of AIF1L Protein?
AIF1L Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1L Protein?
The biological functionality of AIF1L Protein will be determined in the future.

What is the amino acid sequence of AIF1L Protein?
MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.

What applications can AIF1L Protein be used in?
AIF1L Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1L Protein?
The endotoxin level is minimal, AIF1L 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:

Eotaxin Human Recombinant (CCL11), His Tag

Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

Product # :

CHM-344

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Description

Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE

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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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 MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
Background
What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.

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

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

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

What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP

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

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

Who supplies recombinant EOTAXIN 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 EOTAXIN 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:

Osteoprotegerin Mouse Recombinant

Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.

Product # :

CYT-956

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Description

OPG Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 388 amino acids (22-401a.a.) and having a molecular mass of 44.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).OPG is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
Synonyms
Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.
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
ETLPPKYLHY DPETGHQLLC DKCAPGTYLK QHCTVRRKTL CVPCPDHSYT DSWHTSDECV YCSPVCKELQ SVKQECNRTH NRVCECEEGR YLEIEFCLKH RSCPPGSGVV QAGTPERNTV CKKCPDGFFS GETSSKAPCI KHTNCSTFGL LLIQKGNATH DNVCSGNREA TQKCGIDVTL CEEAFFRFAV PTKIIPNWLS VLVDSLPGTK VNAESVERIK RRHSSQEQTF QLLKLWKHQN RDQEMVKKII QDIDLCESSV QRHLGHSNLT TEQLLALMES LPGKKISPEE IERTRKTCKS SEQLLKLLSL WRIKNGDQDT LKGLMYALKH LKTSHFPKTV THSLRKTMRF LHSFTMYRLY QKLFLEMIGN QVQSVKISCL 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:

IFN-Alpha 2b Human Recombinant

IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

Product # :

CYT-205

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Shipped at Room temp

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Description

IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b 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 IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Background
IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.
There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.
The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.
All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.
What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

What is the source or expression system of IFN A 2B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

What is the amino acid sequence of IFN A 2B HUMAN Protein?
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
What applications can IFN A 2B HUMAN Protein be used in?
IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN Protein?
The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 calibrated solution of IFN alpha 2b 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:

Guanine Deaminase Mouse Recombinant

Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.

Product # :

ENZ-1058

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Description

GDA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 477 amino acids (1-454 a.a) and having a molecular mass of 53.4kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDA protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol .

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 4,000 pmol/min/ug, and is defined as
the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37°C.

More Info

Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
Synonyms
Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.
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 MGSMCAARTP PLALVFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE SSQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHAPQ YAFAGSNVDL PLLEWLNKYT FPTEQRFRST DVAEEVYTRV VRRTLKNGTT TACYFGTIHT DSSLILAEIT DKFGQRAFVG KVCMDLNDTV PEYKETTEES VKETERFVSE MLQKNYPRVK PIVTPRFTLS CTETLMSELG NIAKTHDLYI QSHISENREE IEAVKSLYPS YKNYTDVYDK NNLLTNKTVM AHGCYLSEEE LNIFSERGAS IAHCPNSNLS LSSGLLNVLE VLKHKVKIGL GTDVAGGYSY SMLDAIRRAV MVSNVLLINK VNEKNLTLKE VFRLATLGGS QALGLDSEIG NFEVGKEFDA LLINPRASDS PIDLFYGDFV GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

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:

Delta-Like 4 Mouse Recombinant

Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.

Product # :

PRO-2236

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

DLL4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-532 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 512 amino acids and having a molecular mass of 55.8kDa.DLL4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

DLL4 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Delta-Like4, also known as DLL4 is implicated in the Notch signaling pathway as Notch ligand. Consequently DLL4 negatively regulates endothelial cell proliferation, migration as well as angiogenic sprouting. DLL4 is vital for retinal progenitor proliferation and also required for suppressing rod fates in late retinal progenitors and for proper generation of other retinal cell types. Furthermore, at some stage in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.
Synonyms
Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.
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
GSGIFQLRLQ EFVNQRGMLA NGQSCEPGCR TFFRICLKHF QATFSEGPCT FGNVSTPVLG TNSFVVRDKN SGSGRNPLQL PFNFTWPGTF SLNIQAWHTP GDDLRPETSP GNSLISQIII QGSLAVGKIW RTDEQNDTLT RLSYSYRVIC SDNYYGESCS RLCKKRDDHF GHYECQPDGS LSCLPGWTGK YCDQPICLSG CHEQNGYCSK PDECICRPGW QGRLCNECIP HNGCRHGTCS IPWQCACDEG WGGLFCDQDL NYCTHHSPCK NGSTCSNSGP KGYTCTCLPG YTGEHCELGL SKCASNPCRN GGSCKDQENS YHCLCPPGYY GQHCEHSTLT CADSPCFNGG SCRERNQGSS YACECPPNFT GSNCEKKVDR CTSNPCANGG QCQNRGPSRT CRCRPGFTGT HCELHISDCA RSPCAHGGTC HDLENGPVCT CPAGFSGRRC EVRITHDACA SGPCFNGATC YTGLSPNNFV CNCPYGFVGS RCEFPVGLPP SFPWVAHHHH 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:

Keratinocye Growth Factor Mouse Recombinant

HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.

Product # :

CYT-721

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
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biological activity
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Citations

Description

Keratinocyte Growth Factor-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18.9 kDa. The FGF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH-8 and 0.1M NaCl.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant stimulation of KGF-responsive BaF3 indicator cells (measured by 3H-thymidine uptake) is < 10ng/ml corresponding to a specific activity of 100,000 Units/mg.

More Info

Introduction
KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Synonyms
HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 KGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCNDMSPEQT ATSVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNSYNIMEI RTVAVGIVAI KGVESEYYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHSG GEMFVALNQK GIPVKGKKTK KEQKTAHFLP MAIT.

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 Human Respiratory Syncytial Virus

Product # :

ANT-653

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
formulation
purity
More Info
Citations

Description

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

Formulation

* RSV gold conjugation antibody in PBS, PH 7.4.
* RSV capture antibody in PBS, PH 7.4.

Purity

Greater than 95%.

More Info

Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Stability
RSV Paired Antibody although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Lateral flow rapid test.
Type
Mouse antibody Monoclonal.
Purification Method
Purified monoclonal IgG2a 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:

Glia Maturation Factor Beta Mouse Recombinant

Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

Product # :

CYT-006

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMF-beta protein was 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.

More Info

Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta 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 GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
Background
What is the molecular weight/Mw of GMFB MOUSE Protein?
GMFB MOUSE Protein has a total Mw of 16.6kDa.

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

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

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

What is the amino acid sequence of GMFB MOUSE Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

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

What is the endotoxin level for GMFB MOUSE Protein?
The endotoxin level is minimal, GMFB 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:

Decorin Mouse Recombinant

Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.

Product # :

PRO-2234

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH

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:

TRAIL / APO2 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-443

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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biological activity
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Description

TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED₅₀ for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

More Info

Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

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:

LY6C/G, Rat Anti Mouse Antibody

Product # :

ANT-075

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
More Info
Citations

Formulation

1mg/ml in PBS (after reconstitution).

More Info

Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
BM-enriched myeloid cells.
Ig Subclass
Rat IgG2b.
Clone
YRmLy-6C/G.
Applications
Flow cytometry, immunohistochemistry, cell depletion.
This antibody recognizes both Ly-6G and Ly-6C (granulocyte receptor 1- Gr-1). Ly-6G is expressed on most myeloid cells in the bone marrow and all peripheral granulocytes. Ly-6C is also expressed on subsets of lymphocytes and monocytes. For flow cytometry, use 10 µl/106 cells. Exact titer for cell depletion in vivo (cytotoxicity) should be determined by the investigator.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Available Conjugates
This antibody is also available conjugated to biotin and FITC.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A column.

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:

Legumain Mouse Recombinant

Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.

Product # :

ENZ-933

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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sds-page
Citations

Description

LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE HHHHHH.

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:

Elongin B Mouse Recombinant

Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

Product # :

PRO-2550

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

ELOB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 141 amino acids ( 1-118 a.a.) having a molecular mass of 15.6 kDa. The Recombinant Mouse ELOB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains PBS pH-7.4 containing 1mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.
Synonyms
Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.
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 MGSMDVFLMI RRHKTTIFTD AKESSTVFEL KRIVEGILKR PPEEQRLYKD DQLLDDGKTL GECGFTSQTA RPQAPATVGL AFRADDTFEA LRIEPFSSPP ELPDVMKPQD SGGSANEQAV Q

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

Description:

IFN Regulatory Factor-1 Human Recombinant

IRF-1, IRF1, MAR.

Product # :

CYT-449

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
Synonyms
IRF-1, IRF1, MAR.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.

What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.

What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 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:

LY6C/G, Rat Anti Mouse Antibody, FITC

Product # :

ANT-076

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

formulation
More Info
Citations

Formulation

1mg/ml in PBS (after reconstitution).

More Info

Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
BM-enriched myeloid cells.
Ig Subclass
Rat IgG2b.
Clone
YRmLy-6C/G.
Applications
Flow cytometry, immunohistochemistry.
This antibody recognizes both Ly-6G and Ly-6C (granulocyte receptor 1- Gr-1). Ly-6G is expressed on most myeloid cells in the bone marrow and all peripheral granulocytes. Ly-6C is also expressed on subsets of lymphocytes and monocytes. For flow cytometry, use 10 µl/106 cells. Exact titer for IHC should be determined by the investigator.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Available Conjugates
This antibody is also available unconjugated and conjugated to biotin.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A column.

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:

Wingless-Type MMTV Integration Site Family, Member 3A Human Recombinant

Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.

Product # :

CYT-861

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Description

WNT3A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 335 amino acids (19-352 a.a.) and having a molecular mass of 37.5kDa. The WNT3A Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The WNT3A Human protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins are implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. WNT3A is a member of the WNT gene family. WNT3A is a protein which shows 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. The WNT3A gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region.
Synonyms
Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.
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
MSYPIWWSLA VGPQYSSLGS QPILCASIPG LVPKQLRFCR NYVEIMPSVA EGIKIGIQEC QHQFRGRRWN CTTVHDSLAI FGPVLDKATR ESAFVHAIAS AGVAFAVTRS CAEGTAAICG CSSRHQGSPG KGWKWGGCSE DIEFGGMVSR EFADARENRP DARSAMNRHN NEAGRQAIAS HMHLKCKCHG LSGSCEVKTC WWSQPDFRAI GDFLKDKYDS ASEMVVEKHR ESRGWVETLR PRYTYFKVPT ERDLVYYEAS PNFCEPNPET GSFGTRDRTC NVSSHGIDGC DLLCCGRGHN ARAERRREKC RCVFHWCCYV SCQECTRVYD VHTCK.

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:

Thymidylate Synthetase, Mouse Anti Human

TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

Product # :

ANT-002

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluorouracil, 5-fluoro-2-prime-deoxyuridine, and several folate analogs.
Synonyms
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
Immunogen
Anti-human TYMS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TYMS amino acids 1-313 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT1S5AT.
Applications
TYMS antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot and Immunofluorescence analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
TYMS antibody was purified from mouse ascitic fluids by protein-G affinity 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:

Cadherin 5 Mouse Recombinant

Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.

Product # :

PRO-2244

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Description

CDH5 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 583 amino acids (25-599a.a.) and having a molecular mass of 66.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH5 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CDH5 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.
Synonyms
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
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
GPNFPQIDTP NMLPAHHRQK RDWIWNQMHI DEEKNESLPH YVGKIKSNVN RQNAKYVLQG EFAGKIFGVD ANTGNVLAYE RLDREKVSEY FLTALIVDKN TNKNLEQPSS FTVKVHDIND NWPVFSHQVF NASVPEMSAI GTSVIRVTAV DADDPTVAGH ATVLYQIVKG NEYFSIDNSG LIFTKIKNLD REKQAEYKIV VETQDALGLR GESGTATVMI RLEDINDNFP VFTQSTYTFS VPEDIRVGKP LGFLTVVDPD EPQNRMTKYS IMQGEYRDTF TIETDPKRNE GIIKPTKSLD YEVIQQYTFY IEATDPTIRY EYLSSTSGKN KAMVTINVLD VDEPPVFQRH FYHFKLPENQ KKPLIGTVVA KDPDKAQRSI GYSIRKTSDR GQFFRITKQG NIYNEKELDR ETYAWYNLTV EANELDSRGN PVGKESIVQV YIEVLDENDN PPEFAQPYEP KVCENAAQGK LVVQISATDK DVVPVNPKFK FALKNEDSNF TLINNHDNTA NITVKYGQFN REHAKFHYLP VLISDNGVPS LTGTSTLTVG VCKCNEQGEF TFCEEMAAQA GVSIQLEHHH 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.

Description:

Apolipoprotein A-I, Mouse Anti Human

Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

Product # :

ANT-065

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Immunogen
Anti-human APOA1, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human APOA1 amino acids 25-267 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT1E12AT.
Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
APOA1 antibody was purified from mouse ascitic fluids by protein-G affinity 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:

Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 1 Mouse Recombinant

mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor alpha, Camk2n1.

Product # :

PKA-092

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Description

CAMK2N1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa.CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CAMK2N1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).
Synonyms
mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor alpha, Camk2n1.
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 MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQSKRPPKL GQIGRSKRVV IEDDRIDDVL KTMTDKAPPG V.

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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