Search: 649 results found for "superoxide dismutase"

Description:

Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant

HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.

Product # :

ENZ-899

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PAFAH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (1-392 a.a) and having a molecular mass of 46.4kDa.PAFAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PAFAH2 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Platelet-activating factor acetylhydrolase 2 cytoplasmic (PAFAH2) has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. PAFAH2 may share a mutual physiologic function with the plasma-type enzyme.
Synonyms
HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.
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 MGSMGVNQSV GFPPVTGPHL VGCGDVMEGQ NLQGSFFRLF YPCQKAEETM EQPLWIPRYE YCTGLAEYLQ FNKRCGGLLF NLAVGSCRLP VSWNGPFKTK DSGYPLIIFS HGLGAFRTLY SAFCMELASR GFVVAVPEHR DRSAATTYFC KQAPEENQPT NESLQEEWIP FRRVEEGEKE FHVRNPQVHQ RVSECLRVLK ILQEVTAGQT VFNILPGGLD LMTLKGNIDM SRVAVMGHSF GGATAILALA KETQFRCAVA LDAWMFPLER DFYPKARGPV FFINTEKFQT MESVNLMKKI CAQHEQSRII TVLGSVHRSQ TDFAFVTGNL IGKFFSTETR GSLDPYEGQE VMVRAMLAFL QKHLDLKEDY NQWNNLIEGI GPSLTPGAPH HLSSL.

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:

Ubiquitin Conjugating Enzyme E2D2 Human Recombinant, His Tag

ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.

Product # :

ENZ-154

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

UBE2D2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147) and having a molecular mass of 18.9 kDa.The UBE2D2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The UBE2D2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.
Synonyms
ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.
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 MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM.

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:

Carboxypeptidase A4 Human Recombinant

Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.

Product # :

ENZ-942

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CPA4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.
Synonyms
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
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
GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH 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:

Ribonuclease H1 E.Coli Recombinant

Ribonuclease HI, RNase HI, Ribonuclease H, RNase H, rnhA, dasF, herA, rnh, sdrA, b0214, JW0204.

Product # :

ENZ-164

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

RNASEH1 E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155 a.a.) and having a molecular mass of 20kDa.RNASEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RNASEH1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
RNHA is an endonuclease which specifically degrades the RNA of RNA-DNA hybrids. Localized to the nucleus, the RNHA protein mediates the removal of Okazaki fragment RNA primers which are present on the lagging strand during DNA replication. RNHA catalyzes the endonucleolytic cleavage of RNA to a 5'-phosphomonoester and is capable of binding magnesium or manganese as cofactors.
Synonyms
Ribonuclease HI, RNase HI, Ribonuclease H, RNase H, rnhA, dasF, herA, rnh, sdrA, b0214, JW0204.
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 MGSMLKQVEI FTDGSCLGNP GPGGYGAILR YRGREKTFSA GYTRTTNNRM ELMAAIVALE ALKEHCEVIL STDSQYVRQG ITQWIHNWKK RGWKTADKKP VKNVDLWQRL DAALGQHQIK WEWVKGHAGH PENERCDELA RAAAMNPTLE DTGYQVEV.

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:

Beta-Secretase 2 Mouse Recombinant, HEK

BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

Product # :

ENZ-1188

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

More Info

Synonyms
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Physical Appearance
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
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
Background
BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.
Function of BACE2 Protein:
BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.
Implications of BACE2 Protein in Alzheimer's Disease:
Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.
BACE2 Protein and Neuronal Survival:
Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.
Association of BACE2 Protein with Other Neurological Disorders:
Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.
Therapeutic Implications of BACE2 Protein:
Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.
Conclusion:
The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

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:

Leptin Super Antagonist Human Recombinant

Product # :

CYT-1238

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

More Info

Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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:

Coronavirus 2019 3CL Protease Recombinant

Product # :

SARS-058

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Recombinant Coronavirus 2019 3CL Protease having a Mw of approximately 33.8 kDa was purified from E. coli. The CoV-2 3CL contains 306 amino acids and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

CoV-2 3CL solution contains 5 % Trehalose, 0.02 % Tween-20 and PBS, pH 7.4.

Purity

Protein is >98% pure as determined by SDS-PAGE and HPLC analyses.

Biological Activity

CoV-2 3CL is a cysteine protease that cleaves proteins with sequences including LQ(S/A/G). The cleavage takes c-terminal to the glutamine residue.

More Info

Introduction
The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. CoV-2 3CL is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDVVYCPR HVICTSEDML NPNYEDLLIR KSNHNFLVQA GNVQLRVIGH SMQNCVLKLK VDTANPKTPK YKFVRIQPGQ TFSVLACYNG SPSGVYQCAM RPNFTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGN FYGPFVDRQT AQAAGTDTTI TVNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA VLDMCASLKE LLQNGMNGRT ILGSALLEDE FTPFDVVRQC SGVTFQ

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 NS4 Horseradish Peroxidase Recombinant

Product # :

HCV-220

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

The E.coli derived recombinant Horseradish Peroxidase Labeled protein contains the HCV NS4 immunodominant regions.

Source

Escherichia Coli.

Formulation

25mM Tris-HCl pH 8, 1mM EDTA, 1.5M urea & 50%glycerol.

Purity

HCV NS4 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 NS4 a+b HRP although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
HCV NS4 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 NS4 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:

Beta Defensin 116 Human Recombinant

Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

Product # :

CYT-713

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page

Description

DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:

Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.
Introduction:

Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.
Antimicrobial Properties:

BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.
Therapeutic Implications:

The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.
Conclusion:

Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.
What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.

What is the source or expression system of DEFB116 Protein?
Escherichia Coli.

What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.

What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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:

Enoyl CoA Hydratase, Short chain, 1, Mitochondrial, Human Recombinant, Active

Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .

Product # :

ENZ-1046

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a) and having a molecular mass of 30.6kDa. ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ECHS1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% Glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 150 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 umole of crotonoyl-CoA to hydroxybutyryl-CoA per minute per minute at pH 7.5 at 25°C.

More Info

Introduction
ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.
Synonyms
Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .
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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

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:

Ubiquitin Conjugating Enzyme E2M Human Recombinant

NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.

Product # :

ENZ-345

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.
Synonyms
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
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 MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK

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:

Coronavirus 2019 Nucleocapsid (1-419 a.a.), Biotinylated Recombinant

Product # :

SARS-036

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

The HEK293 derived recombinant biotinylated protein contains the Coronavirus 2019 CoV-2 Nucleocapsid, Wuhan-Hu-1 strain, amino acids 1-419 fused to His-Avi tag at C-terminal.

Source

HEK293 Cells.

Formulation

CoV-2 Nucleocapsid protein is supplied in 50mM Tris, 0.15M NaCl & Arginine, pH7.5

Purity

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

More Info

Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cov-2 Nucleocapsid protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Nucleocapsid protein 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.
Purification Method
Purified by Metal-Afinity 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:

Cathepsin-S Mouse Recombinant

Cathepsin S, Ctss, Cats.

Product # :

ENZ-954

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CTSS Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (24-340 a.a.) and having a molecular mass of 36.9kDa.CTSS is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
Synonyms
Cathepsin S, Ctss, Cats.
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
EQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEISCRM GALRISRQSP KTVTFRSYSN RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKAMDE KCHYNSKNRA ATCSRYIQLP FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI LEHHHHHHDY WLVKNSWGLN FGDQGYIRMA RNNKNHCGIA
SYCSYPEILE HHHHHH.

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

Description:

Oncostatin-M Mouse Recombinant

Oncostatin-M, OSM, OncoM.

Product # :

CYT-168

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

More Info

Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
Oncostatin-M, OSM, OncoM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.

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:

Ubiquitin Conjugating Enzyme E2R 2 Human Recombinant

CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.

Product # :

ENZ-511

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

UBE2R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-238 a.a) and having a molecular mass of 29.6kDa (Molecular size on SDS-PAGE will appear higher).UBE2R2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UBE2R2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the ubiquitin-conjugating enzyme family. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase implicated in cell growth andtransformation. This protein is a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies propose that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. UBE2R2 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. UBE2R2 may be implicated in degradation of katenin. Among the diseases associated with UBE2R2 are cblc, and herpes simplex.
Synonyms
CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.
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 MGSMAQQQMT SSQKALMLEL KSLQEEPVEG FRITLVDESD LYNWEVAIFG PPNTLYEGGY FKAHIKFPID YPYSPPTFRF LTKMWHPNIY ENGDVCISIL HPPVDDPQSG ELPSERWNPT QNVRTILLSV ISLLNEPNTF SPANVDASVM FRKWRDSKGK DKEYAEIIRK QVSATKAEAE KDGVKVPTTL AEYCIKTKVP SNDNSSDLLY DDLYDDDIDD EDEEEEDADC YDDDDSGNEE S

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

Description:

Carbohydrate Sulfotransferase 5 Human Recombinant

Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.

Product # :

ENZ-1165

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

CHST5 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (27-395 a.a.) and having a molecular mass of 42.9kDa.CHST5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CHST5 protein solution (0.25mg/ml) containing 20% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is greater than 10,000 pmol/min/ug, and is defined as the amount of enzyme that sulfate from PAPS to Nacetyl-D-glucosamine per minute at pH 7.5, at 37˚C.

More Info

Introduction
Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.
Synonyms
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
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
ADPEFSRQVP SSPAGLGERV HVLVLSSWRS GSSFVGQLFS QHPDVFYLME PAWHVWDTLS QGSAPALHMA VRDLIRSVFL CDMDVFDAYL PWRRNISDLF QWAVSRALCS PPVCEAFARG NISSEEVCKP LCATRPFGLA QEACSSYSHV VLKEVRFFNL QVLYPLLSDP ALNLRIVHLV RDPRAVLRSR EQTAKALARD NGIVLGTNGT WVEADPRLRV VNEVCRSHVR IAEAALHKPP PFLQDRYRLV RYEDLARDPL TVIRELYAFT GLGLTPQLQT WIHNITHGSG PGARREAFKT TSRDALSVSQ AWRHTLPFAK IRRVQELCGG ALQLLGYRSV HSELEQRDLS LDLLLPRGMD SFKWASSTEK QPESHHHHHH

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:

Granzyme-K, Human Recombinant, sf9

GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.

Product # :

ENZ-1031

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

GZMK Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 247 amino acids (27-264) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMK is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GZMK protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

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

More Info

Introduction
GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.
Synonyms
GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.
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
ADPIIGGKEV SPHSRPFMAS IQYGGHHVCG GVLIDPQWVL TAAHCQYRFT KGQSPTVVLG AHSLSKNEAS KQTLEIKKFI PFSRVTSDPQ SNDIMLVKLQ TAAKLNKHVK MLHIRSKTSL RSGTKCKVTG WGATDPDSLR PSDTLREVTV TVLSRKLCNS QSYYNGDPFI TKDMVCAGDA KGQKDSCKGD SGGPLICKGV FHAIVSGGHE CGVATKPGIY TLLTKKYQTW IKSNLVPPHT NHHHHHH.

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:

Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant

Enoyl-CoA hydratase 1, SCEH.

Product # :

ENZ-556

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ECHS1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT,0.1M NaCl and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.
Synonyms
Enoyl-CoA hydratase 1, SCEH.
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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

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 Synuclein NACP112 Human Recombinant

Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

Product # :

PRO-162

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.

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:

Phosphopantothenoylcysteine Decarboxylase Human Recombinant

FLJ14585, PPC-DC, MDS018, COAC, CoaC, Phosphopantothenoylcysteine Decarboxylase.

Product # :

ENZ-011

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PPCDC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (1-204a.a.) and having a molecular mass of 24.6kDa.PPCDC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PPCDC protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer(pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
PPCDC is a member of the HFCD (homo oligomeric flavin containing Cys decarboxylase) superfamily which takes a part in the biosynthesis of coenzyme A (CoA) from pantothenate (Vitamin B). The biosynthesis of CoA from pantothenate needs several steps: the phosphorylation of pantothenate, the conversion of 4’-hosphopantothenate to 4''-phosphopantetheine, the adenylation by phosphopantetheine adenylyltransferase to form dephospho-CoA and the phosphorylation by dephospho-CoA kinase to form CoA. PPCDC is a key player in this pathway. PPCDC converts 4''-phosphopantothenate into 4''-phosphopantetheine.
Synonyms
FLJ14585, PPC-DC, MDS018, COAC, CoaC, Phosphopantothenoylcysteine Decarboxylase.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEPKASCPAA APLMERKFHV LVGVTGSVAA LKLPLLVSKL LDIPGLEVAV VTTERAKHFY SPQDIPVTLY SDADEWEMWK SRSDPVLHID LRRWADLLLV APLDANTLGK VASGICDNLL TCVMRAWDRS KPLLFCPAMN TAMWEHPITA QQVDQLKAFG YVEIPCVAKK LVCGDEGLGA MAEVGTIVDK VKEVLFQHSG FQQS

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:

Formiminotransferase Cyclodeaminase Human Recombinant

Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.

Product # :

ENZ-302

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

Formiminotransferase Cyclodeaminase Human Recombinant (also called liver cytosol type 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 59,749 Dalton.The FTCD is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

FTCD is supplied in 16mM HEPES buffer pH-7.6, 240mM sodium chloride, and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.
Synonyms
Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°Cfor longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels, immuno-dot test).
coating concentration
0.35-0.7 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

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:

Beta Defensin-3 Human Recombinant

HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

Product # :

CYT-461

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HBD-3 was lyophilized without additives.

Purity

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

More Info

Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 Beta Defensin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
Background
Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy
Abstract:

Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.
Introduction:

The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.
Properties and Mode of Action:

hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.
Production of hBD-3 Human Recombinant:

Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.
Applications and Future Perspectives:

hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.
Conclusion:

hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 5.1kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
The biological functionality of BD3 Protein will be determined in the future.

What is the amino acid sequence of BD3 Protein?
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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:

Bartter Syndrome Infantile with Sensorineural Deafness Human Recombinant

Bartter Syndrome Infantile With Sensorineural Deafness (Barttin) , Deafness Autosomal Recessive 73, DFNB73, BART, barttin.

Product # :

PRO-1551

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BSND Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 290 amino acids (54-320) and having a molecular mass of 31.7kDa.BSND is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BSND solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
BSND is a vital beta subunit for CLC chloride channels. These heteromeric channels are restricted to basolateral membranes of renal tubules and of potassium-secreting epithelia of the inner ear. BSND gene mutations are linked with Bartter syndrome with sensorineural deafness.
Synonyms
Bartter Syndrome Infantile With Sensorineural Deafness (Barttin) , Deafness Autosomal Recessive 73, DFNB73, BART, barttin.
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 MGSCQCYPKI TFVPADSDFQ GILSPKAMGL LENGLAAEMK SPSPQPPYVR LWEEAAYDQS LPDFSHIQMK VMSYSEDHRS LLAPEMGQPK LGTSDGGEGG PGDVQAWMEA AVVIHKGSDE SEGERRLTQS WPGPLACPQG PAPLASFQDD LDMDSSEGSS PNASPHDREE ACSPQQEPQG CRCPLDRFQD FALIDAPTLE DEPQEGQQWE IALPNNWQRY PRTKVEEKEA SDTGGEEPEK EEEDLYYGLP DGAGDLLPDK ELGFEPDTQG

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:

Hexokinase-4 Human Recombinant, Active

Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.

Product # :

PKA-116

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

GCK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.3kDa. GCK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GCK protein solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 2,000 pmol/min/ug. One unit will convert 1 pmoles of D-Glucose to D-Glucose-6-phosphate per minute at pH8.0 at 37C.

More Info

Introduction
GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.
.
Synonyms
Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.
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 MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.

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

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

sds-page

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info