Search: 810 results found for "tumor necrosis factor"

Description:

Interleukin-12 Human Recombinant

NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-101

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Shipping Method :

Shipped at Room temp

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Description

Interleukin-12 Human Recombinant produced in HEK cells is a glycosylated heterodimer, having a total molecular weight of 57kDa.The IL12 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

IL12 was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
The EC₅₀ is 0.5ng/ml.

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.
Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL12 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 IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
>IL-12 A
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
>IL-12B
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.
Background
What is the molecular weight/Mw of IL12 HUMAN Protein?
IL12 HUMAN Protein has a total Mw of 57kDa.

What is the source or expression system of IL12 HUMAN Protein?
HEK.

What is the Purity of IL12 HUMAN Protein?
IL12 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 HUMAN Protein?
The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
The EC50 is 0.5ng/ml.
What is the amino acid sequence of IL12 HUMAN Protein?
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
>IL-12 A
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
>IL-12B
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.

What applications can IL12 HUMAN Protein be used in?
IL12 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 HUMAN Protein?
The endotoxin level is minimal, IL12 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 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 IL12 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-12 Mouse Recombinant

NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-144

Price :

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Shipped at Room temp

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Description

Interleukin-12 Mouse Recombinant produced in HEK 293 cells is a glycosylated disulfide linked heterodimeric polypeptide containing 506 amino acids and having a molecular weight of 75 kDa comprised of disulfide-bonded 35 kDa (p35) and 40 kDa (p40) subunits.The IL-12 is purified by proprietary chromatographic techniques.

Source

HEK-293 Cells.

Formulation

The protein was lyophilized from 0.5xPBS, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

IL-12 Mouse has full biological activity when compared to standards. The ED₅₀ is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x10⁵ units/mg.

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 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 murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.
Background
What is the molecular weight/Mw of IL12 MOUSE Protein?
IL12 MOUSE Protein has a total Mw of 75kDa.

What is the source or expression system of IL12 MOUSE Protein?
HEK-293 Cells.

What is the Purity of IL12 MOUSE Protein?
IL12 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 MOUSE Protein?
IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

What is the amino acid sequence of IL12 MOUSE Protein?
p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.
p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

What applications can IL12 MOUSE Protein be used in?
IL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 MOUSE Protein?
The endotoxin level is minimal, IL12 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 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 IL12 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:

Hypoxia-Inducible Factor-1 Alpha Human Recombinant

Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

Product # :

PRO-477

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Shipped with Ice Packs

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Description

HIF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (530-826) and having a molecular mass of 32.8kDa. The protein migrates as a 32.8kDa band on SDS-PAGE. The HIF1-A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HIF1A recombinant Human solution (1mg/ml) is formulated in PBS pH-7.4 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Hypoxia-inducible factor-1 (HIF-1), identified as one of the transcription factors, has been found to play an essential role in cellular and systemic oxygen homeostasis. HIF-1 is a heterodimer composed of HIF-1b subunit and one of three subunits (Hif-1a, Hif-2 (or Hif-3)). The activation of Hif-1 (is closely associated with a variety of tumors and oncogenic pathways. Hif-1 (consists of DNA binding domain (DBD domain), Dimerization domain and C-terminal regulatory domains, including two transactivation domains (TAD), an oxygen-dependent degradation (ODD) domain, and inhibitory domains. Under hypoxic conditions HIF1A activates the transcription of more than 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, VEGF, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1A also plays a crucial role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. It binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation involves recruitment of transcriptional coactivators such as CREBPB and EP300. Its activity is improved by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX appears to activate CTAD and potentiates activation by NCOA1 and CREBBP. The induction is under reduced oxygen tension. HIF1A is also induced by a variety of receptor-mediated factors such as growth factors, cytokines, and circulatory factors for example PDGF, EGF, FGF-2, IGF-2, TGF-1 beta, HGF, TNF alpha, IL-1 beta, angiotensin-2 and thrombin. Nevertheless, this induction is less intense than that stimulated by hypoxia.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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
MEFKLELVEK LFAEDTEAKN PFSTQDTDLD LEMLAPYIPM DDDFQLRSFD QLSPLESSSA SPESASPQST VTVFQQTQIQ EPTANATTTT ATTDELKTVT KDRMEDIKIL IASPSPTHIH KETTSATSSP YRDTQSRTAS PNRAGKGVIE QTEKSHPRSP NVLSVALSQR TTVPEEELNP KILALQNAQR KRKMEHDGSL FQAVGIGTLL QQPDDHAATT SLSWKRVKGC KSSEQNGMEQ KTIILIPSDL ACRLLGQSMD ESGLPQLTSY DCEVNAPIQG SRNLLQGEEL LRALDQVN.

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

Description:

Interleukin-3 Receptor Subunit Alpha Mouse Recombinant

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

Product # :

CYT-1210

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Shipped with Ice Packs

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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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

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

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

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

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

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

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

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

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

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

Description:

Monocyte Chemotactic Protein-1 Rat 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, Immediate-early serum-responsive JE protein.

Product # :

CHM-315

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Quantity :

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Shipped at Room temp

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Description

Monocyte Chemotactic Protein-1 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 125 amino acids and having a molecular mass of 14.1 kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

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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 weightof 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, Immediate-early serum-responsive JE protein.
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-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.
Background
What is the molecular weight/Mw of CCL2 RAT Protein?
CCL2 RAT Protein has a total Mw of 14.1kDa.

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

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

What is the Biological Activity of CCL2 RAT Protein?
ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

What is the amino acid sequence of CCL2 RAT Protein?
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.

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

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

Who supplies recombinant CCL2 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 CCL2 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Neurotrophic Receptor Tyrosine Kinase 3 Mouse Recombinant

NT-3 growth factor receptor, GP145-TrkC, Trk-C, Neurotrophic tyrosine kinase receptor type 3, TrkC tyrosine kinase, Ntrk3, TrkC, AW125844, Ntrk3_tv3

Product # :

CYT-1163

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Shipped with Ice Packs

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Description

NTRK3 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 404 amino acids (32-429 aa) and having a molecular mass of 45.4kDa.NTRK3 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NTRK3 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Neurotrophic Receptor Tyrosine Kinase 3 (NTRK3)belongs to the receptor tyrosine kinases family and is a high affinity catalytic receptor of neurotrophin NT-3. NTRK3 mediates multiple effects of this neurotrophic factor, which includes neuronal differentiation and survival. NTRK3 inducesvarious pleiotorpic responses in malignant cells, including enhanced tumor cell invasiveness and chemotoxis.Increased NTRK3 expression was observed in neuroblastoma, medulloblastoma, and in neuroectodermal brain tumors.
Synonyms
NT-3 growth factor receptor, GP145-TrkC, Trk-C, Neurotrophic tyrosine kinase receptor type 3, TrkC tyrosine kinase, Ntrk3, TrkC, AW125844, Ntrk3_tv3
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
CPANCVCSKT EINCRRPDDG NLFPLLEGQD SGNSNGNASI NITDISRNIT SIHIENWRGL HTLNAVDMEL YTGLQKLTIK NSGLRNIQPR AFAKNPHLRY INLSSNRLTT LSWQLFQTLS LRELRLEQNF FNCSCDIRWM QLWQEQGEAR LDSQSLYCIS ADGSQLPLFR MNISQCDLPE ISVSHVNLTV REGDNAVITC NGSGSPLPDV DWIVTGLQSI NTHQTNLNWT NVHAINLTLV NVTSEDNGFT LTCIAENVVG MSNASVALTV YYPPRVVSLV EPEVRLEHCI EFVVRGNPTP TLHWLYNGQP LRESKIIHMD YYQEGEVSEG CLLFNKPTHY NNGNYTLIAK NALGTANQTI NGHFLKEPFP ESTDFFDFES DASPTPPITV THKPEEDTHH 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:

Stromal Cell-Derived Factor-1 alpha Rat Recombinant (CXCL12)

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

Product # :

CHM-354

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Description

Stromal Cell-Derived Factor-1 alpha Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9 kDa. The SDF-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXCL12 protein was lyophilized from a concentrated (1 mg/ml) sterile solution 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

The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100 ng/ml.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SDF-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.
Background
What is the molecular weight/Mw of CXCL12 RAT ALPHA Protein?
CXCL12 RAT ALPHA Protein has a total Mw of 7.9kDa.

What is the source or expression system of CXCL12 RAT ALPHA Protein?
Escherichia Coli.

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

What is the Biological Activity of CXCL12 RAT ALPHA Protein?
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

What is the amino acid sequence of CXCL12 RAT ALPHA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.

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

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

Who supplies recombinant CXCL12 RAT ALPHA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL12 RAT ALPHA?
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:

ADP-Ribosylation Factor 1 Human Recombinant

ARF-1, ADP-ribosylation factor 1.

Product # :

PRO-867

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Description

ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.
Synonyms
ARF-1, ADP-ribosylation factor 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
MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.

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 10 Receptor Alpha Human Recombinant

Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

Product # :

CYT-892

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Description

IL10RA Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated, polypeptide chain containing 220 amino acids (22-235 a.a.) and having a molecular mass of 25.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IL10RA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL10RA protein solution (0.2mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN Protein?
IL10RA HUMAN Protein has a total Mw of 25.2kDa.

What is the source or expression system of IL10RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL10RA HUMAN Protein?
IL10RA HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RA HUMAN Protein?
The biological functionality of IL10RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL10RA HUMAN Protein?
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH.

What applications can IL10RA HUMAN Protein be used in?
IL10RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10RA HUMAN Protein?
The endotoxin level is minimal, IL10RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10RA 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 IL10RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-1 Receptor Antagonist Human Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

Product # :

CYT-203

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Description

IL1ra Human Recombinant produced in E.Coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton. The IL1ra is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized protein with no additives.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1 ra in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
Background
What is the molecular weight/Mw of IL 1RA HUMAN Protein?
IL 1RA HUMAN Protein has a total Mw of 17kDa.

What is the source or expression system of IL 1RA HUMAN Protein?
Escherichia Coli.

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

What is the Biological Activity of IL 1RA HUMAN Protein?
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.

What is the amino acid sequence of IL 1RA HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.

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

What is the endotoxin level for IL 1RA HUMAN Protein?
The endotoxin level is minimal, IL 1RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 1RA HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 1RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 ra 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:

Tissue Plasminogen Activator Human Recombinant

Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

Product # :

ENZ-263

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Quantity :

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Description

Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a molecular mass of 59008.71 Dalton. tPA is a serine protease enzyme that converts plasminogen to plasmin. The tPA is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells (CHO)

Formulation

Each mg of t-PA contains 1.7 gr L-arginine, 0.5 gr phosphoric acid and 4 mg tween 80.

Purity

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

More Info

Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA 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 t-PA in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Enzymatic Activity
580,000 IU/mg.

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:

Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Product # :

CYT-1121

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Description

Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque 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 Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.

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

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

What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.

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

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

Mitochondrial Ribosome Recycling Factor Human Recombinant

MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

Product # :

PRO-1299

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Description

MRRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (56-262 a.a.) and having a molecular mass of 25.1kDa.MRRF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MRRF protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.
Synonyms
MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.
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 MATKKAKAKG KGQSQTRVNI NAALVEDIIN LEEVNEEMKS VIEALKDNFN KTLNIRTSPG SLDKIAVVTA DGKLALNQIS QISMKSPQLI LVNMASFPEC TAAAIKAIRE SGMNLNPEVE GTLIRVPIPQ VTREHREMLV KLAKQNTNKA KDSLRKVRTN SMNKLKKSKD TVSEDTIRLI EKQISQMADD TVAELDRHLA VKTKELLG.

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:

Sulfatase Modifying Factor 1 Human Recombinant

Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.

Product # :

PRO-986

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Description

SUMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (91-374 a.a.) and having a molecular mass of 34.1kDa.SUMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

SUMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2M UREA, 2mM DTT and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.
Synonyms
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
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 MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE TSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD

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, Rat Anti-Mouse

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

Product # :

ANT-166

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Quantity :

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Formulation

1mg/ml in PBS (after reconstitution).

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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 I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.mouse IFN-g.
Ig Subclass
rat IgG1.
Clone
NYRmIFNg.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Intracellular staining.
Titer
By direct ELISA, 1:8,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange.

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:

Omentin Human Recombinant

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Product # :

CYT-301

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.

Source

E.Coli.

Formulation

Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.

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:

Hepatoma-Derived Growth Factor-2 Human Recombinant

Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

Product # :

CYT-132

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.
Synonyms
Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.
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 MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.
Background
What is the molecular weight/Mw of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

What is the source or expression system of HDGF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGF2 HUMAN Protein?
The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

What applications can HDGF2 HUMAN Protein be used in?
HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGF2 HUMAN Protein?
The endotoxin level is minimal, HDGF2 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:

Interferon Regulatory Factor-7, Mouse Anti Human

Interferon regulatory factor 7, IRF-7, IRF7.

Product # :

ANT-418

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

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

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Introduction
IRF7 belongs to the interferon regulatory transcription factor (IRF) family. IRF7 plays a role in the transcriptional activation of virus-inducible cellular genes, including interferon beta chain genes. Inducible expression of IRF7 is largely restricted to lymphoid tissue.
Synonyms
Interferon regulatory factor 7, IRF-7, IRF7.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human IRF7 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human IRF7 amino acids 1-150 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P3D9AT.
Applications
IRF7 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 analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.
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
IRF7 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:

Granulocyte Colony Stimulating Factor, Mouse Anti-Human, FITC

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

ANT-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
More Info
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Formulation

1 mg/ml in PBS (after reconstitution).

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene.
Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human G-CSF.
Ig Subclass
Mouse IgG.
Clone
NYRhGCSF.
Applications
Direct ELISA, Western Blot, Intra-cellular staining.
Titer
For intra-cellular staining use 10µl per 1,000,000 cells.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human 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.

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:

Cerebral Neurotrophic Factor Human Recombinant

Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

Product # :

CYT-167

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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 CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L
Background
Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology
The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.
Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.
The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.
Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.
In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

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

What is the Purity of CDNF Protein?
CDNF Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

What is the amino acid sequence of CDNF Protein?
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

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

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

Von Hippel-Lindau Protein Human Recombinant

Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.

Product # :

PRO-440

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Recombinant Human Von Hippel-Lindau Protein b-domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) & having a molecular mass of 19.2 kDa. The Von Hippel-Lindau antigen is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.

Source

Escherichia Coli.

Formulation

The Von Hippel-Lindau Protein contains 1x PBS pH-7.4, 2mM EDTA, and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).
Synonyms
Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.
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 MPRRAENWDE AEVGAEEAGV EEYGPEEDGG EESGAEESGPEESGPEELGA EEEMEAGRPR PVLRSVNSRE PSQVIFCNRS PRVVLPVWLN FDGEPQPYPT LPPGTGRRIH SYRGHLWLFR DAGTHDGLLV NQTELFVPSL NVDGQPIFAN ITLP.

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:

Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity of FLT1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for this effect is typically 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 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 FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.

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-11 Human Recombinant

AGIF, Adipogenesis inhibitory factor, IL-11.

Product # :

CYT-214

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Interleukin-11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19256.29 Dalton. The IL-11 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

More Info

Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
Synonyms
AGIF, Adipogenesis inhibitory factor, IL-11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 11 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 Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IL11 HUMAN Protein?
IL11 HUMAN Protein has a total Mw of 19.25kDa.

What is the source or expression system of IL11 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL11 HUMAN Protein?
IL11 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL11 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

What is the amino acid sequence of IL11 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.

What applications can IL11 HUMAN Protein be used in?
IL11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL11 HUMAN Protein?
The endotoxin level is minimal, IL11 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL11 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 IL11 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.95 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 IL-11 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:

Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 Human Recombinant

Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

Product # :

PRO-1898

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

AIFM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (98-609) and having a molecular mass of 58.5 kDa.AIFM1 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIFM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.
Synonyms
Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 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
MGSSHHHHHH SSGLVPRGSH MGSEFLGLTP EQKQKKAALS ASEGEEVPQD KAPSHVPFLL IGGGTAAFAA ARSIRARDPG ARVLIVSEDP ELPYMRPPLS KELWFSDDPN VTKTLRFKQW NGKERSIYFQ PPSFYVSAQD LPHIENGGVA VLTGKKVVQL DVRDNMVKLN DGSQITYEKC LIATGGTPRS LSAIDRAGAE VKSRTTLFRK IGDFRSLEKI SREVKSITII GGGFLGSELA CALGRKARAL GTEVIQLFPE KGNMGKILPE YLSNWTMEKV RREGVKVMPN AIVQSVGVSS GKLLIKLKDG RKVETDHIVA AVGLEPNVEL AKTGGLEIDS DFGGFRVNAE LQARSNIWVA GDAACFYDIK LGRRRVEHHD HAVVSGRLAG ENMTGAAKPY WHQSMFWSDL GPDVGYEAIG LVDSSLPTVG VFAKATAQDN PKSATEQSGT GIRSESETES EASEITIPPS TPAVPQAPVQ GEDYGKGVIF YLRDKVVVGI VLWNIFNRMP IARKIIKDGE QHEDLNEVAK LFNIHED.

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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