Search: 1000 results found for "HTLV"

Description:

Leucine Zipper Transcription Factor-Like 1 Human Recombinant

Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

Product # :

PRO-2157

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.
Synonyms
Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 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 MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.

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:

6-Pyruvoyltetrahydropterin Synthase Human Recombinant

PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.

Product # :

ENZ-471

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

More Info

Introduction
6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.
Synonyms
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
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 MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.

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:

Sorbin And SH3 Domain Containing 3 Human Recombinant

Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

Product # :

PRO-1829

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.
Synonyms
Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.
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 MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV

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:

Endoglin Human Recombinant, His-Tag

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

Product # :

CYT-823

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

More Info

Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.

What is the source or expression system of CD105 Protein?
Escherichia Coli.

What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.

What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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:

TNF-Related Apoptosis Inducing Ligand/Apo2L Mouse Recombinant

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

Product # :

CYT-806

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

TRAIL Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.2kDa.

Source

Escherichia Coli.

Formulation

The protein was lyophilized containing PBS, pH 7.4, and 3mM DTT.

Purity

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

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2,000,000 IU/mg in the presence of actinomycin D.

More Info

Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TRAIL although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TRAIL recombinant 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 TRAIL Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPRGGRPQKV AAHITGITRR SNSALIPISK DGKTLGQKIE SWESSRKGHS FLNHVLFRNG ELVIEQEGLY YIYSQTYFRF QEAEDASKMV SKDKVRTKQL VQYIYKYTSY PDPIVLMKSA RNSCWSRDAE YGLYSIYQGG LFELKKNDRI FVSVTNEHLM DLDQEASFFG AFLIN

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-31 Canine Recombinant, HEK

IL-31, Interleukin 31, IL31.

Product # :

CYT-1215

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Synonyms
IL-31, Interleukin 31, IL31.
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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.

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 NS3 47.8kDa Recombinant

Product # :

HCV-010

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Recombinant HCV NS3 Genotype 1a produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 47.8kDa and fused to a His tag at N-terminus.

Source

Escherichia Coli.

Formulation

Lyophilized from 1mg/ml in 20mM sodium carbonate pH-9.6.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
HCV NS3 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HCV NS3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Lymphotoxin-alpha, Mouse Anti Human

Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.

Product # :

ANT-014

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

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

More Info

Introduction
Lymphotoxin-alpha (LT-alpha or LTA) belongs to the TNF ligand superfamily, which bind the same TNF receptor and mediate similar pleiotropic effect. LTA is a proinflammatory cytokine with important biological activity and immunomodulatory function and is known to influence a variety of cellular response. Furthermore, LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses, is involved in the formation of secondary lymphoid organs during development and has a role in apoptosis. LTA is highly inducible, secreted, and forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA, which is located within the MHC III region of chromosome 6, shows close relation to the HLA class I (HLA-B) and class II (HLA-DR) genes. Polymorphism in the LTA gene appears to contribute to infectious disease susceptibility and infection. Genetic variations in the LTA gene are linked to susceptibility to leprosy type 4 and psoriatic arthritis.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human LTA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LTA amino acids 35-205 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and ? light chain.
Clone
PAT15A3AT.
Applications
LTA antibody has been tested by ELISA, Western blot and Immunofluorescence 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 and Immunofluorescence is 1:250 ~ 500.
Recommended starting dilution is 1:250.
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
LTA 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:

Coagulation Factor VIIa Human Recombinant

Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.

Product # :

PRO-331

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Factor VIIa Human Recombinant produced in BHK is a glycosylated polypeptide two-chain dimer consisting of 406 amino acids with a molecular weight of 50kD.The Factor-VIIa is purified by proprietary chromatographic techniques.

Source

BHK cells (Baby Hamster Kidney Cells).

Formulation

The protein 1 mg/ml was lyophilized after from a sterile solution containing 10mg sucrose pH-6.

Purity

Greater than 98.0% as determined by analysis by SDS-PAGE.

Biological Activity

The potency per mg was tested and found to be 50,000Units/mg.

More Info

Introduction
Coagulation factor VII is a vitamin K-dependent factor which is essential for hemostasis. It circulates in the blood as a zymogen which is later converted to an active form by factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of factor VII, a heavy chain with a catalytic domain and a light chain with 2 EGF-like domains are generated, and the two chains are held together by a disulfide bond. The presence of factor III and calcium ions further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of factor VII results in 2 transcripts. Defects in coagulation factor VII can cause coagulopathy. Coagulation factor VII initiates the extrinsic pathway of blood coagulation. Minor proteolysis converts factor VII to factor VIIa by factors Xa, XIIa, IXa, or thrombin. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium.
Synonyms
Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Factor-VIIa although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIIa 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 Factor-VIIa in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Prolactin Human Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-267

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Prolactin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 23007 Dalton. The Prolactin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.

Purity

Greater than 95.0% 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 the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065ng/ml corresponding to a Specific Activity of 15,385,000IU/mg.

More Info

Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin 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-Leu-Pro-Ile-Cys.

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:

Growth Hormone Antagonist Ovine Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-215

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Somatotropin Ovine Antagonist Recombinant G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. The Somatotropin Ovine Antagonist Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3, pH 9.

Purity

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

Biological Activity

GH G119R acts as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD) and binds to this ECD with affinity similar the the wild type oGH.

More Info

Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH G119R although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 GH G119R in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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:

Brain-Derived Neurotrophic Factor Human Recombinant

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-207

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Activity
Citations

Description

BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

Purity

BDNF is greater than 950% as determined SDS-PAGE.

Biological Activity

The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

Activity

More Info

Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.

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

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

What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 Brain-derived Neurotrophic Factor 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:

TROVE Domain Family Member 2 Human Recombinant, Biotinlyated

60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

Product # :

PRO-2561

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

Source

Bovine tissues.

Formulation

TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.

Purity

Greater than 83.0% as determined by SDS-PAGE.

More Info

Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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.

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:

Human Follicle Stimulating Hormone

Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.

Product # :

HOR-249

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
More Info
Citations

Description

FSH Human is a glycoprotein produced from urine of post-menopausal women and having a total molecular mass of 30,000 Dalton.FSH is a heterodimeric hormone consisting of 92 amino acids a chain and 111 amino acids b chain.The FSH is purified by proprietary chromatographic techniques.

Source

Urine of post-menopausal women.

Formulation

The FSH was lyophilized with no additives.

More Info

Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone(GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads.
Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Follicle Stimulating Hormone in sterile pyrogen free water at 2,000IU/1ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein has a total Mw of 30kDa.

What is the source or expression system of FOLLICLE STIMULATING HORMONE HUMAN Protein?
Urine of post-menopausal women.

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

What is the amino acid sequence of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein is composed from 92 amino acids a chain and 111 amino acids b chain.

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

What is the endotoxin level for FOLLICLE STIMULATING HORMONE HUMAN Protein?
The endotoxin level is minimal, FOLLICLE STIMULATING HORMONE HUMAN Protein was purified using conventional chromatography techniques.
Contaminants
Less than: 0.1% hCG, 0.5%TSH, 0.5% LH, 0.5%GH and 0.5%Prl.Free of HbsAg, antibodies to HIV and HCV.

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:

Respiratory Syncytial Virus Human Recombinant

Product # :

RSV-001

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Recombinant Human Respiratory Syncytial Virus produced in E. coli having a Mw of 44kDa. RSV Human is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

RSV protein solution contains 0.25% sodium azide, 10mM K2CO3 and PBS.

Purity

Protein is >90% pure as determined by 10% PAGE (coomassie staining).

More Info

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
HMALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFT GLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEI QINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVI RRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAG LFMNAYGAGQV MLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHIL NNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGV
Background
Respiratory Syncytial Virus (RSV) remains a formidable pathogen, especially in vulnerable populations such as infants and the elderly, causing significant morbidity and mortality worldwide. The pursuit of effective preventive and therapeutic strategies has led to the exploration of RSV Recombinant Protein as a key player in the molecular battle against this respiratory pathogen. This research aims to unravel the intricacies of RSV Recombinant Protein, shedding light on its structural features, immunogenic potential, and its applications in vaccine development and antiviral therapies. By dissecting the properties of RSV Recombinant Protein, scientists seek to fortify our defenses against RSV and advance the prospects for improved clinical outcomes.
Structural Insights into RSV Recombinant Protein:
RSV Recombinant Protein, engineered to mimic key viral antigens, offers a controlled and standardized tool for studying the virus's structural components. Understanding the protein's three-dimensional structure and conformational characteristics is paramount for elucidating its interactions with the immune system, guiding the design of effective vaccines, and unraveling potential targets for antiviral drugs.
Immunogenic Potential and Vaccine Development:
The quest for an effective RSV vaccine has been challenged by the virus's ability to elude natural immunity. RSV Recombinant Protein, designed to trigger robust immune responses, is a promising candidate for vaccine development. By presenting viral antigens to the immune system in a controlled manner, the recombinant protein aims to induce protective immune responses, particularly neutralizing antibodies, that guard against RSV infection and its associated complications.
Application in Passive Immunization and Therapeutics:
Beyond vaccination, RSV Recombinant Protein holds promise in the realm of passive immunization and antiviral therapies. Monoclonal antibodies derived from the recombinant protein can be employed to provide immediate, targeted immunity against RSV. This approach is particularly relevant for individuals at high risk, such as premature infants or immunocompromised patients, offering a bridge to protection until their own immune responses can be activated.
Challenges and Future Directions:
While RSV Recombinant Protein represents a beacon of hope in the fight against RSV, challenges persist. The virus's ability to mutate and evade immune detection necessitates ongoing research to refine and adapt recombinant strategies. Additionally, considerations of vaccine safety, optimal dosing, and potential side effects demand thorough investigation to ensure the translational success of RSV Recombinant Protein-based interventions.
RSV Recombinant Protein emerges as a key protagonist in the scientific narrative against Respiratory Syncytial Virus. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies mark it as a pivotal tool in our arsenal. As researchers continue to decipher the molecular intricacies of RSV Recombinant Protein, they pave the way for innovative strategies that may revolutionize RSV prevention and treatment, ultimately shaping the landscape of respiratory virus control and global health.

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:

Herpes Simplex Virus-2 VP13/14 Recombinant

Product # :

HSV-227

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

The E.Coli derived HSV-2 VP13/14 recombinant protein, 1-280 amino acids, is fused to a Six histidine tag at C-terminus and has a MW of 31kDa (pI 6.77).

Source

Escherichia Coli.

Formulation

10 mM Phosphate buffer pH 7.6; 75 mM NaCl.

Purity

Protein is >90% pure as determined by SDS PAGE.

More Info

Introduction
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
Physical Appearance
Sterile Filtered clear solution.
Stability
HSV-2 VP13/14 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
ELISA, WB, Flow-Through.

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 Core 22kDa, FLSCN Recombinant

Product # :

HCV-261

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
formulation
purity
More Info
Citations

Description

The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-192. The FLSCN labeled protein is fused with b-galactosidase (114 kDa) at N-terminus.

Formulation

20mM Tris-Hcl pH 8, 8M urea and 10mM B-ME.

Purity

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

More Info

Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Stability
HCV-Core although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
HCV-Core antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV-Core protein was purified by proprietary chromatographic technique.

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

Description:

Nucleolin Human Recombinant

Nucleolin, Protein C23, NCL, C23.

Product # :

PRO-1508

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.
Synonyms
Nucleolin, Protein C23, NCL, C23.
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.

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:

Cathepsin L, Mouse Anti Human

Cathepsin L1, EC 3.4.22.15, Major excreted protein, MEP, CTSL1, CTSL, CATL, FLJ31037.

Product # :

ANT-384

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

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

More Info

Introduction
Cathepsins B, C, H, L, S, V, X/Z/P and 1 are cysteine proteases of the papain family. Cathepsin C is also known as DPPI (dipeptidyl-peptidase I). Cathepsin A is a serine carboxypeptidase and Cathepsin D and E are aspartic proteases. As lysosomal proteases, cathepsins play an important role in protein degradation. Because of their redistribution or increased levels in human and animal tumors, cathepsins may have a role in invasion and metastasis. Cathepsins are synthesized as inactive proenzymes and processed to become mature and active enzymes. Endogenous protein inhibitors, such as cystatins and some serpins, inhibit active enzymes.
Synonyms
Cathepsin L1, EC 3.4.22.15, Major excreted protein, MEP, CTSL1, CTSL, CATL, FLJ31037.
Immunogen
Anti-human Cathepsin-L mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cathepsin-L amino acids 114-333 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
P2H7AT.
Applications
Cathepsin-L 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
Cathepsin-L 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:

Growth Hormone Polyclonal Rabbit Anti Human Antibody

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

ANT-036

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
purity
More Info
Citations

Formulation

Lyophilized from a sterile filtered (0.2µm) solution containing phosphate buffered saline.

Purity

Greater than 98%.

More Info

Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Stability
Store at -20°C. For long term storage freezes in working aliquots at -20°C. Repeated freezing and thawing is not recommended.
Solubility
Add distilled water at 1:2 ratio and let the lyophilized pellet dissolve completely.
Immunogen
IgG Anti HGH has been developed in rabbit using highly pure (>98%) recombinant human HGH expressed in plants.
Applications
ELISA: to detect HGH by indirect ELISA, a dilution of at least 1/1,000 of this antibody is required. This antibody, in conjunction with compatible secondary reagents (anti rabbit AP conjugated), allows the detection of 0.2-1 ng/well of HGH.
Western Blot: to detect HGH by WB analysis this antibody can be used in a dilution of 1/1,500.
Antigen Amino Acid Sequence
FPTI PLSRLFDNAM LRAHRLHQLAFDTYQ EFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNRE ETQQKSNLE LLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLL KDLEEGIQTLMGRLE DGSPRTGQIFKQ TYSK DTNSHNDDALLKNYGLLYCFRK DM DKVETFLRIVQCRSVEGSCGF
Type
Polyclonal Rabbit Antibody.
Purification Method
Purified IgG prepared by affinity chromatography on protein G.

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:

Adiponectin Human Recombinant, HEK

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-434

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
sds-page
Citations

Description

Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

Purity

Greater than 98% as determined by HPLC and SDS PAGE.

Biological Activity

In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

sds-page

More Info

Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
For long term, store lyophilized AdipoQ at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized protein remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.

What is the source or expression system of adiponectin Protein?
HEK293.

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

What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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

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

Histidine Triad Nucleotide Binding Protein 2 Human Recombinant

Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.

Product # :

PRO-1455

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

HINT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (18-163 a.a) and having a molecular mass of 17.9kDa.HINT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HINT2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Histidine triad nucleotide-binding protein 2 (HINT2) belongs to the triad proteins, which are nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides. Hydrolase is most likely involved in steroid biosynthesis, furthermore it might play a role in apoptosis. HINT2 shows high expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients.
Synonyms
Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.
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 MGSVAATGVR GGQVRGAAGV TDGNEVAKAQ QATPGGAAPT IFSRILDKSL PADILYEDQQ CLVFRDVAPQ APVHFLVIPK KPIPRISQAE EEDQQLLGHL LLVAKQTAKA EGLGDGYRLV INDGKLGAQS VYHLHIHVLG GRQLQWPPG.

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:

Alpha-2-HS-Glycoprotein Mouse Recombinant

Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.

Product # :

PRO-2220

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

AHSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 333 amino acids (19-345.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). AHSG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

AHSG protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.
Synonyms
Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.
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
APQGTGLGFR ELACDDPEAE QVALLAVDYL NNHLLQGFKQ VLNQIDKVKV WSRRPFGVVY EMEVDTLETT CHALDPTPLA NCSVRQLTEH AVEGDCDFHI LKQDGQFRVM HTQCHSTPDS AEDVRKLCPR CPLLTPFNDT NVVHTVNTAL AAFNTQNNGT YFKLVEISRA QNVPLPVSTL VEFVIAATDC TAKEVTDPAK CNLLAEKQHG FCKANLMHNL GGEEVSVACK LFQTQPQPAN ANAVGPVPTA NAALPADPPA SVVVGPVVVP RGLSDHRTYH DLRHAFSPVA SVESASGETL HSPKVGQPGA AGPVSPMCPG RIRHFKIHHH HHH.

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

Description:

AITR Human Recombinant

TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.

Product # :

CYT-925

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

AITR Human Recombinant produced in Sf9 Baculovirus is a single, glycosylated polypeptide chain containing 145 amino acids (26-162a.a.) and having a molecular mass of 15.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).AITR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

More Info

Synonyms
TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.
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
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.
Background
AITR Human Recombinant: Unveiling its Role in Immune Regulation and Therapeutic Potential
1. Abstract
This research paper aims to provide a comprehensive exploration of the AITR Human Recombinant, a crucial receptor involved in immune regulation. By examining its structure, signaling pathways, biological functions, and implications in disease, we unravel the potential therapeutic applications of AITR in immune-related disorders.
2. Introduction
AITR, also known as TNFRSF18, is a receptor protein that plays a vital role in immune regulation. With its involvement in T-cell responses and immune tolerance, AITR has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITR
AITR is a transmembrane receptor protein belonging to the tumor necrosis factor receptor superfamily. Its extracellular domain interacts with its ligand, glucocorticoid-induced TNFR-related protein (GITR) ligand, leading to downstream signaling events that modulate immune cell function.
4. Biological Functions of AITR
AITR activation influences T-cell responses by regulating T-cell activation, proliferation, and cytokine production. Additionally, AITR signaling can modulate the balance between effector and regulatory T-cell populations, thereby playing a role in immune tolerance and immune homeostasis.
5. AITR in Disease Pathology
AITR dysregulation has been associated with various immune-related disorders, including autoimmune diseases, cancer, and transplant rejection. Understanding the role of AITR in these pathologies may provide insights into potential therapeutic strategies targeting AITR signaling.
6. Therapeutic Potential of AITR
The unique role of AITR in immune regulation makes it an appealing target for therapeutic interventions. Modulation of AITR signaling holds promise for manipulating immune responses in the context of autoimmune diseases, cancer immunotherapy, and transplantation.
7. Conclusion and Future Perspectives
While our understanding of AITR and its functions has advanced significantly, further research is warranted to unravel its complex signaling pathways and therapeutic potential. Continued investigations into AITR biology will enhance our ability to develop targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITR Protein?
AITR Protein has a total Mw of 15.6kDa.

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

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

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

What is the amino acid sequence of AITR Protein?
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.

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

What is the endotoxin level for AITR Protein?
The endotoxin level is minimal, AITR 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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

sds-page

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Formulation

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations