Search: 1000 results found for "influenza"

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:

Borrelia Afzelii Outer Surface Protein C Recombinant

Product # :

BOR-016

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Description

Recombinant Borrelia Afzelii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 22,151 Dalton. Borrelia Afzelii OspC is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

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

Description:

Coagulation Factor III Mouse Recombinant

Tissue factor, TF, Coagulation factor III, CD142.

Product # :

PRO-2316

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Description

F3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (29-251 a.a.) and having a molecular mass of 26.4kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). F3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

F3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.
Synonyms
Tissue factor, TF, Coagulation factor III, CD142.
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
ADPAGIPEKA FNLTWISTDF KTILEWQPKP TNYTYTVQIS DRSRNWKNKC FSTTDTECDL TDEIVKDVTW AYEAKVLSVP RRNSVHGDGD QLVIHGEEPP FTNAPKFLPY RDTNLGQPVI QQFEQDGRKL NVVVKDSLTL VRKNGTFLTL RQVFGKDLGY IITYRKGSST GKKTNITNTN EFSIDVEEGV SYCFFVQAMI FSRKTNQNSP GSSTVCTEQW KSFLGEHHHH 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:

Interleukin-36 Alpha 153 a.a Mouse Recombinant

Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

Product # :

CYT-181

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Description

IL36A 153 a.a. Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (8-160a.a.) and having a molecular mass of 17.0kDa.The IL36A 153 a.a. Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2?m filtered concentrated solution in 1xPBS, pH 7.4 and 5% trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-6 secretion in NIH-3T3 mouse embryonic fibroblast cells is less than 20ng/ml, corresponding to a specific activity of 50,000IU/mg.

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Introduction
Murine IL-36a belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.
Synonyms
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36A 153 a.a. Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 153 a.a. Mouse 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 IL36A 153 a.a. Mouse in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH

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:

Glucokinase E.coli Recombinant, BioActive

Glucokinase, ECK2384, JW2385.

Product # :

PKA-121

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Description

GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GLK protein solution (1mg/ml) contains 0.15M NaCl, 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 70unit/mg obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. One unit will oxidize 1.0 umole of Glucose to D-glucose 6-phosphate per minute in the presence of Beta-NADP at pH 9.0 at 37C.

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Introduction
Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.
Synonyms
Glucokinase, ECK2384, JW2385.
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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL

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

Description:

Macrophage Inflammatory Protein-3 Human Recombinant (CCL23)

C-C motif chemokine 23, Small-inducible cytokine A23, Macrophage inflammatory protein 3, Myeloid progenitor inhibitory factor 1, CK-beta-8, MIP-3, MPIF-1, CKB-8, CCL23, MIP3, MPIF1, SCYA23, CKb8, Ckb-8-1.

Product # :

CHM-358

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Description

MIP-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 99 amino acids and having a molecular mass of 11.3kDa. The MIP-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract human T cell population using a concentration range of 10-50ng/ml corresponding to a Specific Activity of 20,000-100,000IU/mg.

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Introduction
CCL23 (MIP-3) is a ligand for the CCR1chemokine receptor. CCL23 is one of several cytokine genes clustered on the q-arm of chromosome 17, in a locus containing several other CC chemokines. MIP-3 chemoattracts monocytes, resting T-lymphocytes and neutrophils, but not activated lymphocytes. Furthermore, it was shown that MIP-3 inhibits colony formation of bone marrow myeloid immature progenitors. MIP-3 is mainly expressed in lung and liver tissue, but can be also found in bone marrow and placenta, as well as in some cell lines of myeloid origin.
Alternative splicing of the CCL23 gene produces 2 mRNAs which encode a short (CK?8) and a long (CK?81) isoform of the MIP-3. CK?8 cDNA encodes a 120 amino acid residue precursor protein with a putative 21 a.a. residue signal peptide which is cleaved to generate a 99 a.a. residue mature CK?8 (a.a. 22-120). Further N-terminal processing of the 99 a.a. residue variant can produce a 75 a.a. residue CK?8 (a.a. 46-120) which is considerably more active than the 99 a.a. residue variant.
MIP-3 may be involved in the malignant progression of certain human cancer cells which overexpress ErbB2 through the transactivation of ErbB2 tyrosine kinase. MIP-3 may also be involved in angiogenesis via upregulation of matrix metalloproteinase MMP-2 expression.
Synonyms
C-C motif chemokine 23, Small-inducible cytokine A23, Macrophage inflammatory protein 3, Myeloid progenitor inhibitory factor 1, CK-beta-8, MIP-3, MPIF-1, CKB-8, CCL23, MIP3, MPIF1, SCYA23, CKb8, Ckb-8-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL23 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MIP-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR SIPCSLLESYFETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN.
Background
What is the molecular weight/Mw of CCL23 HUMAN Protein?
CCL23 HUMAN Protein has a total Mw of 11.3kDa.

What is the source or expression system of CCL23 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL23 HUMAN Protein?
CCL23 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL23 HUMAN Protein?
Determined by its ability to chemoattract human T cell population using a concentration range of 10-50ng/ml corresponding to a Specific Activity of 20,000-100,000IU/mg.

What is the amino acid sequence of CCL23 HUMAN Protein?
RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR SIPCSLLESYFETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN.

What applications can CCL23 HUMAN Protein be used in?
CCL23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL23 HUMAN Protein?
The endotoxin level is minimal, CCL23 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL23 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 CCL23 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:

I-TAC Human Recombinant (CXCL11), His Tag

Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

Product # :

CHM-232

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Description

I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
Synonyms
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
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 MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.
Background
What is the molecular weight/Mw of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein has a total Mw of 10.6kDa.

What is the source or expression system of CXCL11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL11 HUMAN, HIS Protein?
The biological functionality of CXCL11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.

What applications can CXCL11 HUMAN, HIS Protein be used in?
CXCL11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL11 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL11 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL11 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 CXCL11 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:

Polyclonal Rabbit Anti Dengue 3 NS1

Product # :

ANT-085

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Description

The polyclonal antibody to dengue serotype 3 NS1 was collected from the rabbit immunized with full length recombinant dengue serotype 3 NS1 antigen, reactive to all dengue serotype NS1.

Source

Rabbit.

Formulation

200mM glycine, pH 7.5 and 0.02% NaN3.

Purity

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

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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.
Isotype
Purified IgG.
Purification Method
Purified 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:

Hepatitis C Virus Cocktail Recombinant

Product # :

HCV-015

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Description

Recombinant HCV cocktail contains the recombinant hepatitis C virus core, NS3, NS4, NS5 proteins.

Source

Escherichia Coli.

Formulation

HCV Cocktail solution contains 25mM K2CO3 and PBS.

Purity

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

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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.
Applications
ELISA and lateral flow immunoassay.
Background
Hepatitis C virus (HCV) is a major global health concern, with approximately 71 million people infected worldwide. Chronic HCV infection can lead to liver cirrhosis, hepatocellular carcinoma, and other severe liver-related complications. The nonstructural proteins NS3, NS4, and NS5 of HCV play critical roles in viral replication, assembly, and immune evasion, making them attractive targets for antiviral interventions. This research aims to characterize the recombinant forms of HCV NS3, NS4, and NS5 proteins to gain insights into their functional properties and identify potential targets for the development of effective antiviral strategies.
The primary objective of this study is to express and purify recombinant HCV NS3, NS4, and NS5 proteins using suitable expression systems. Recombinant DNA techniques will be employed to generate expression vectors harboring the respective genes, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant proteins will be purified using affinity chromatography or other appropriate methods, enabling subsequent biochemical and biophysical characterization.
The second objective is to investigate the roles of NS3, NS4, and NS5 proteins in HCV replication and assembly. In vitro assays will be performed to assess the enzymatic activities of NS3 protease and NS5 RNA-dependent RNA polymerase (RdRp). The effects of potential inhibitors or small molecules on these enzymatic activities will be evaluated. Furthermore, the interactions between NS4 protein and cellular components involved in viral assembly will be explored using protein-protein interaction assays.
The third objective is to determine the three-dimensional structures of the recombinant NS3, NS4, and NS5 proteins using techniques such as X-ray crystallography or cryo-electron microscopy. Structural information will provide valuable insights into the functional domains and potential binding sites within these proteins. These findings will aid in the design of novel antiviral compounds targeting specific regions of NS3, NS4, and NS5, with the goal of disrupting viral replication and assembly.
By characterizing the recombinant forms of HCV NS3, NS4, and NS5 proteins, this research aims to enhance our understanding of the molecular mechanisms underlying HCV infection. The insights gained from this study may contribute to the development of novel antiviral strategies targeting HCV, ultimately leading to improved therapeutic options for individuals affected by this persistent and debilitating viral infection.

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

Description:

HIV-1 p30 Recombinant

Product # :

HIV-016

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Description

Recombinant HIV-1 p30 produced in E. coli having a Mw of 30kDa. Recombinant HIV-1 p30 is fused to a 6xHis tag at its C-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

HIV-1 p30 solution contains 25mM K2₂CO₃ & PBS.

Purity

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

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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.
Applications
ELISA, WB & LFA.
Background
HIV-1 p30, a multifunctional regulatory protein encoded by the Human Immunodeficiency Virus type 1 (HIV-1), has drawn considerable attention due to its critical roles in viral replication and pathogenesis. While HIV research has traditionally focused on better-known viral proteins like gp120 and reverse transcriptase, the significance of p30 in the HIV lifecycle and its potential as a therapeutic target have become increasingly evident. This study aims to provide a comprehensive exploration of HIV-1 p30, shedding light on its various functions and potential applications in understanding and combatting HIV/AIDS.
The primary objective of this research is to elucidate the multifaceted roles of HIV-1 p30 in viral replication and pathogenesis. In vitro and in vivo experiments will be conducted to investigate the protein's interactions with host cellular factors, its influence on viral transcription, and its impact on immune evasion. Understanding these mechanisms is crucial for unraveling the complexities of HIV-1 infection.
The second objective is to assess the clinical relevance of HIV-1 p30 in HIV/AIDS progression. Clinical studies involving HIV-infected individuals will be conducted to evaluate the correlation between p30 expression levels and disease progression. These investigations may provide insights into the potential use of p30 as a prognostic marker and therapeutic target in HIV/AIDS management.
The third objective is to explore the therapeutic implications of targeting HIV-1 p30. Research will investigate the development of novel antiretroviral agents or immunotherapies that specifically target p30-mediated processes, such as viral latency and immune suppression. Harnessing the potential of p30 as a therapeutic target may lead to innovative approaches in the fight against HIV/AIDS.

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:

Inhibin-Alpha A Chain Human Recombinant

Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

Product # :

HOR-293

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Description

Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Synonyms
Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein has a total Mw of 19.2kDa.

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

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

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

What is the amino acid sequence of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein is composed from 134 amino acids.

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

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

Who supplies recombinant INHIBIN 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 INHIBIN 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:

Dengue-2 Envelope Hydrophobic Domain Recombinant

Product # :

DEN-039

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Description

The Recombinant Dengue 2 Envelope Hydrophobic Domain e.coli derived contains 225 amino acids (228-485) from dengue 2 envelope. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

Source

E.coli.

Formulation

PBS.

Purity

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

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Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
Physical Appearance
Sterile Filtered clear solution.
Stability
Dengue 2 Envelope Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Immunoassay.

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 Mouse Recombinant

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

Product # :

CYT-371

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Description

Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 should be stored at 4°C between 2-7 days and for future use below -18°C.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-3 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 Met-Asp-Thr-His-Arg.
Background
What is the molecular weight/Mw of IL3 MOUSE Protein?
IL3 MOUSE Protein has a total Mw of 15.1kDa.

What is the source or expression system of IL3 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL3 MOUSE Protein?
IL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

What is the amino acid sequence of IL3 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

What applications can IL3 MOUSE Protein be used in?
IL3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 MOUSE Protein?
The endotoxin level is minimal, IL3 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 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 IL3 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 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 IL3 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:

Interleukin-5 Mouse Recombinant

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.

Product # :

CYT-689

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Description

Interleukin-5 Mouse Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 2 x 113 amino acids forming a disulfide linked homodimer and having a molecular mass of 26.2 kDa.The Mouse IL-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 20mM Sodium Phosphate and 50mM NaCl pH-7.5.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/mg.

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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse Interleukin-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse IL5 should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Mouse Interleikin-5 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.
Background
What is the molecular weight/Mw of IL 5 MOUSE Protein?
IL 5 MOUSE Protein has a total Mw of 26.2kDa.

What is the source or expression system of IL 5 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL 5 MOUSE Protein?
IL 5 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/mg.

What is the amino acid sequence of IL 5 MOUSE Protein?
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.

What applications can IL 5 MOUSE Protein be used in?
IL 5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Who supplies recombinant IL 5 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 5 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:

HIV-1 Tat Interactive Protein 2, Mouse Anti Human

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

Product # :

ANT-522

Price :

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Formulation

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

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Introduction
HTATIP2 is part of the short-chain dehydrogenases/reductases (SDR) family which acts as a tumor suppressor in metabolic suppression, inhibition of angiogenesis and induces the expression of apoptosis related genes Bad and Siva. HTATIP2 cooperates with the activation domain of HIV-1 TAT and enhances its transcription by phosphorylating RNA polymerase II (Pol II). Defects in HTATIP2 are related with hepatocellular carcinomas and apoptotic resistant tumor cells, implicating a probable use for HTATIP2 in antitumor therapy.
Synonyms
TIP30, CC3, SDR44U1, HTATIP2, EC=1.1.1.-, HIV-1 TAT-interactive protein 2, FLJ26963.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human HTATIP2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HTATIP2 amino acids 1-242 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and ? light chain.
Clone
PAT5D6AT.
Applications
HTATIP2 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
HTATIP2 antibody was purified from mouse ascitic fluids by protein-A 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:

Monoclonal Mouse Anti Dengue NS1

Product # :

ANT-495

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Description

Paired monoclonal antibodies developed for dengue NS1 antigen test by lateral flow immunoassay device. First antibody is for conjugation and the second antibody is for membrane coating. Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibody solutions (100µg in total).

Formulation

*Dengue NS1 Antibody solution for gold conjugation (3.6mg/ml) in PBS and Sodium nitrate.

*Dengue NS1 Antibody solution for membrane coating (2.2mg/ml) in PBS and Sodium nitrate.

Purity

95% pure (12% SDS-PAGE and Coomassie staining).

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Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Applications
Lateral flow immunoassay.
Assay Conditions
1. 1-2 days fresh prepared gold particle with maximal homogeneity in gold particle size, λ 525-529, OD 1.2-1.4. 2. Conjugation at pH 8.5, conjugation time should be 6-8 hours. 3. Blocking condition: remove supernatant and re-suspend gold pellet bound with anti-dengue NS1 to OD 8.0- 8.2, add casein to the final 0.3-0.4%. 4. Treat sample pad with 50mM sodium borate, 0.5% mouse serum and 0.5% Triton X-100, pH8.0.
Purification Method
Purified monoclonal IgG by protein A chromatography.

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

Description:

IFN Regulatory Factor-5 Human Recombinant

IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

Product # :

CYT-816

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SDS-PAGE
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Description

IRF5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (176-240a.a) and having a molecular mass of 10.7kDa.IRF5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IRF5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.
Synonyms
IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I
Background
What is the molecular weight/Mw of IRF5 HUMAN Protein?
IRF5 HUMAN Protein has a total Mw of 10.7kDa.

What is the source or expression system of IRF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF5 HUMAN Protein?
IRF5 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF5 HUMAN Protein?
The biological functionality of IRF5 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF5 HUMAN Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

What applications can IRF5 HUMAN Protein be used in?
IRF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF5 HUMAN Protein?
The endotoxin level is minimal, IRF5 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:

Cytomegalo Virus gB Recombinant

Product # :

CMV-211

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Description

The E.Coli derived recombinant artificial mosaic protein contains the CMV gB immunodominant regions 11-67 amino acids, fused with a 26 kDa GST Tag, the protein weight is 6.5kDa, having a total weight of 32.5 kDa.

Source

Escherichia Coli.

Formulation

50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.

Purity

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

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Introduction
MV belongs to the Beta herpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods.CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
Stability
CMV gB protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Specificity
Immunoreactive with sera of CMV-infected individuals.
Purification Method
CMV gB was purified by proprietary chromatographic technique.

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

Description:

Borrelia Garinii OspC Recombinant

Product # :

BOR-021

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Description

Recombinant Borrelia Garinii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 22kDa.Borrelia Garinii OspC is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Borrelia Garinii OspC is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

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

Description:

Interleukin-6 Rat Recombinant, sf9

IL6, Ifnb2, ILg6.

Product # :

CYT-1048

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Description

IL6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (25-211 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL6 protein solution (0.5mg/ml) contains 20% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IL6, Ifnb2, ILg6.
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
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH
Background
Production and Applications of Rat Recombinant Interleukin-6 in sf9 Cells
Abstract:
Interleukin-6 (IL-6) is a critical cytokine involved in various physiological processes, including inflammation, immune responses, and hematopoiesis. The production of recombinant IL-6 has paved the way for numerous applications in research and therapeutic development. This paper elucidates the production of Rat Recombinant IL-6 in sf9 cells using baculovirus expression system and explores its potential applications in immunology and disease research.
Introduction:
Interleukin-6 is a pleiotropic cytokine with diverse functions in immune regulation, acute phase responses, and tissue homeostasis. The ability to produce recombinant IL-6 allows researchers to investigate its role in various biological contexts and develop potential therapies. The sf9 cell line, derived from Spodoptera frugiperda insect cells, offers an efficient platform for recombinant protein expression through the baculovirus system.
Methods:
The production of Rat Recombinant IL-6 involves inserting the rat IL-6 gene into a baculovirus transfer vector. This vector is then co-transfected with a linearized baculovirus DNA into sf9 cells. The resulting recombinant baculovirus expresses the IL-6 protein, which is secreted into the culture medium. The expressed protein is subsequently purified using chromatographic techniques to ensure its quality and activity.
Applications:
Rat Recombinant IL-6 produced in sf9 cells has widespread applications. It serves as a valuable tool for investigating the mechanisms underlying IL-6-mediated immune responses, inflammation, and hematopoiesis. Furthermore, it enables the development of potential therapies targeting IL-6-related disorders, including autoimmune diseases, inflammatory conditions, and certain types of cancer.
Advantages of sf9 Expression:
The sf9 expression system offers several advantages, including high protein yields, post-translational modifications, and proper protein folding. This system is especially suitable for complex cytokines like IL-6, which require correct tertiary structure for optimal biological activity.
Challenges and Future Prospects:
While sf9-based expression of Rat Recombinant IL-6 offers numerous benefits, challenges such as optimization of expression conditions, scale-up, and quality control remain. Additionally, further research is needed to explore the therapeutic potential of Rat Recombinant IL-6 in preclinical and clinical settings.
Conclusion:
The production of Rat Recombinant IL-6 in sf9 cells using the baculovirus expression system provides a powerful tool for unraveling the roles of IL-6 in various biological processes. This platform holds promise for advancing our understanding of IL-6-related diseases and facilitating the development of targeted therapeutic interventions.
What is the molecular weight/Mw of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein has a total Mw of 22.8kDa.

What is the source or expression system of IL6 RAT, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 RAT, SF9 Protein?
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

What is the amino acid sequence of IL6 RAT, SF9 Protein?
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH.

What applications can IL6 RAT, SF9 Protein be used in?
IL6 RAT, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6 RAT, SF9 Protein?
The endotoxin level is minimal, IL6 RAT, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6 RAT, SF9 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 IL6 RAT, SF9?
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 4 Human Recombinant, Yeast

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

Product # :

CYT-712

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.The IL-4 is purified by proprietary chromatographic techniques.

Source

Pichia pastoris.

Formulation

The protein was lyophilized from 0.2µm filtered solution in 20mM sodium phosphate buffer pH 6.0 in absence of any carrier protein.

Purity

Greater than 98% as determined by SDS-PAGE.

Biological Activity

The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED₅₀ = 0.05–0.4ng/ml.

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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin-4 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 Interleukin-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the source or expression system of IL 4 HUMAN, YEAST Protein?
Pichia pastoris.

What is the Purity of IL 4 HUMAN, YEAST Protein?
IL 4 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 HUMAN, YEAST Protein?
The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED50 = 0.05–0.4ng/ml.

What is the amino acid sequence of IL 4 HUMAN, YEAST Protein?
IL 4 HUMAN, YEAST Protein is composed from 129 amino acids.

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

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

Who supplies recombinant IL 4 HUMAN, YEAST that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 4 HUMAN, YEAST?
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:

Endothelial-Monocyte Activating Polypeptide II Human Recombinant

AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

Product # :

CYT-607

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

Purity

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

Biological Activity

Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II 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 EMAP-II in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.

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

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

What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

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

Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag

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

Product # :

CHM-345

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.

What is the source or expression system of CXCL8 HUMAN, HIS Protein?
Escherichia Coli.

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

What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.

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

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

Who supplies recombinant CXCL8 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 CXCL8 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:

Isovaleryl Coenzyme A Dehydrogenase Human Recombinant

FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.

Product # :

ENZ-490

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The IVD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.
Synonyms
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
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 MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.

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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